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- PDB-7nhk: LsaA, an antibiotic resistance ABCF, in complex with 70S ribosome... -

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Basic information

Entry
Database: PDB / ID: 7nhk
TitleLsaA, an antibiotic resistance ABCF, in complex with 70S ribosome from Enterococcus faecalis
Components
  • (30S ribosomal protein ...) x 19
  • (50S ribosomal protein ...) x 28
  • 16S rRNA
  • 23S rRNA
  • 5S rRNA
  • ABC-F type ribosomal protection protein Lsa(A)
  • RNA (5'-R(P*GP*GP*AP*GP*GP*UP*AP*UP*GP*AP*CP*AP*A)-3')
  • tRNA-fMETi
KeywordsRIBOSOME / Antibiotic resistance element / ribosomal protein / LsaA / ABCF / target protection / antibiotic resistance
Function / homology
Function and homology information


regulation of translation / large ribosomal subunit / ribosome biogenesis / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding ...regulation of translation / large ribosomal subunit / ribosome biogenesis / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / ATP hydrolysis activity / RNA binding / zinc ion binding / ATP binding / cytoplasm / cytosol
Similarity search - Function
Ribosomal protein L31 type B / : / : / : / Type-1 KH domain profile. / Ribosomal protein L1, bacterial-type / : / Ribosomal protein S14, type Z / Ribosomal protein L1, conserved site / Ribosomal protein L1 signature. ...Ribosomal protein L31 type B / : / : / : / Type-1 KH domain profile. / Ribosomal protein L1, bacterial-type / : / Ribosomal protein S14, type Z / Ribosomal protein L1, conserved site / Ribosomal protein L1 signature. / Ribosomal protein L1 / Ribosomal protein L1, 3-layer alpha/beta-sandwich / Ribosomal protein L1-like / Ribosomal protein L1/ribosomal biogenesis protein / Ribosomal protein L1p/L10e family / Ribosomal protein L31 signature. / Ribosomal protein L31 / Ribosomal protein L31 superfamily / Ribosomal protein L31 / Ribosomal protein L16 signature 1. / Ribosomal protein L16 signature 2. / Ribosomal protein L16, conserved site / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / : / Ribosomal protein L17 signature. / Ribosomal protein L36 signature. / Ribosomal protein L32p, bacterial type / Ribosomal protein L28/L24 superfamily / : / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / Ribosomal protein L28 / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L18, bacterial-type / : / ABC transporter-like, conserved site / ABC transporters family signature. / Ribosomal protein L6, bacterial-type / Ribosomal protein S3, bacterial-type / Ribosomal protein S14/S29 / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein L5, bacterial-type / Ribosomal protein S4, bacterial-type / Ribosomal protein L36 / Ribosomal protein L36 superfamily / Ribosomal protein L36 / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein L19, conserved site / Ribosomal protein L19 signature. / Ribosomal protein L27, conserved site / Ribosomal protein L27 signature. / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein L20 signature. / Ribosomal protein L22, bacterial/chloroplast-type / Ribosomal protein L14P, bacterial-type / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal protein L34, conserved site / Ribosomal protein L34 signature. / Ribosomal protein L2, bacterial/organellar-type / Ribosomal protein L35 / Ribosomal protein L35 superfamily / Ribosomal protein L35 / Ribosomal protein L33 / Ribosomal protein L18 / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / Ribosomal protein L33 / Ribosomal L28 family / Ribosomal protein L33 superfamily / Ribosomal protein S9, bacterial/plastid / Ribosomal protein L16 / Ribosomal protein S18, conserved site / Ribosomal protein L28/L24 / Ribosomal protein S18 signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / Ribosomal protein S16 / Ribosomal protein L30, bacterial-type / Ribosomal protein S16 domain superfamily / Ribosomal protein S16 / L28p-like / : / Ribosomal protein S15, bacterial-type / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein L27 / Ribosomal protein S6 superfamily / Ribosomal L27 protein / Ribosomal protein S12, bacterial-type / Ribosomal protein L20
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / : / 1,4-DIAMINOBUTANE / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 ...ADENOSINE-5'-TRIPHOSPHATE / : / 1,4-DIAMINOBUTANE / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Small ribosomal subunit protein bS18 / Small ribosomal subunit protein bS6 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein uS12 / Large ribosomal subunit protein uL3 / Small ribosomal subunit protein uS10 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein uL23 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS19 / Large ribosomal subunit protein uL14 / Large ribosomal subunit protein uL5 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS8 / Large ribosomal subunit protein uL18 / Small ribosomal subunit protein uS14 / Large ribosomal subunit protein uL15 / Large ribosomal subunit protein uL22 / Small ribosomal subunit protein uS13 / Large ribosomal subunit protein bL36 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL29 / Small ribosomal subunit protein uS11 / Large ribosomal subunit protein uL24 / Small ribosomal subunit protein uS5 / Large ribosomal subunit protein uL30 / Large ribosomal subunit protein bL17 / Large ribosomal subunit protein bL35 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein bL27 / Large ribosomal subunit protein bL21 / Large ribosomal subunit protein bL32 / Large ribosomal subunit protein bL31B / Small ribosomal subunit protein bS16 / Large ribosomal subunit protein bL19 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein bS20 / Large ribosomal subunit protein uL1 / Large ribosomal subunit protein bL33 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS15 / Large ribosomal subunit protein bL28 / Small ribosomal subunit protein uS9 / Large ribosomal subunit protein uL13 / Large ribosomal subunit protein bL34 / 50S ribosomal protein L6 / 50S ribosomal protein L4 / ABC-F type ribosomal protection protein Lsa(A)
Similarity search - Component
Biological speciesEnterococcus faecalis (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsCrowe-McAuliffe, C. / Kasari, M. / Hauryliuk, V.H. / Wilson, D.N.
Funding support Germany, Sweden, Estonia, 6items
OrganizationGrant numberCountry
German Research Foundation (DFG)WI3285/8-1 Germany
Swedish Research Council2017-03783 Sweden
Swedish Research Council2019-01085 Sweden
European Regional Development Fund2014-2020.4.01.15-0013 Sweden
Estonian Research CouncilPRG335 Estonia
Swedish Research Council2018-00956 Sweden
CitationJournal: Nat Commun / Year: 2021
Title: Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens.
Authors: Caillan Crowe-McAuliffe / Victoriia Murina / Kathryn Jane Turnbull / Marje Kasari / Merianne Mohamad / Christine Polte / Hiraku Takada / Karolis Vaitkevicius / Jörgen Johansson / Zoya ...Authors: Caillan Crowe-McAuliffe / Victoriia Murina / Kathryn Jane Turnbull / Marje Kasari / Merianne Mohamad / Christine Polte / Hiraku Takada / Karolis Vaitkevicius / Jörgen Johansson / Zoya Ignatova / Gemma C Atkinson / Alex J O'Neill / Vasili Hauryliuk / Daniel N Wilson /
Abstract: Target protection proteins confer resistance to the host organism by directly binding to the antibiotic target. One class of such proteins are the antibiotic resistance (ARE) ATP-binding cassette ...Target protection proteins confer resistance to the host organism by directly binding to the antibiotic target. One class of such proteins are the antibiotic resistance (ARE) ATP-binding cassette (ABC) proteins of the F-subtype (ARE-ABCFs), which are widely distributed throughout Gram-positive bacteria and bind the ribosome to alleviate translational inhibition from antibiotics that target the large ribosomal subunit. Here, we present single-particle cryo-EM structures of ARE-ABCF-ribosome complexes from three Gram-positive pathogens: Enterococcus faecalis LsaA, Staphylococcus haemolyticus VgaA and Listeria monocytogenes VgaL. Supported by extensive mutagenesis analysis, these structures enable a general model for antibiotic resistance mediated by these ARE-ABCFs to be proposed. In this model, ABCF binding to the antibiotic-stalled ribosome mediates antibiotic release via mechanistically diverse long-range conformational relays that converge on a few conserved ribosomal RNA nucleotides located at the peptidyltransferase center. These insights are important for the future development of antibiotics that overcome such target protection resistance mechanisms.
History
DepositionFeb 10, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 5, 2021Provider: repository / Type: Initial release
Revision 1.1Jun 23, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Jul 10, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_admin
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_admin.last_update

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Structure visualization

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  • Deposited structure unit
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Structure viewerMolecule:
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Assembly

Deposited unit
0: ABC-F type ribosomal protection protein Lsa(A)
1: 50S ribosomal protein L29
2: 50S ribosomal protein L30
4: 50S ribosomal protein L32
5: 50S ribosomal protein L33
6: 50S ribosomal protein L34
7: 50S ribosomal protein L35
8: 50S ribosomal protein L36
A: 23S rRNA
B: 5S rRNA
G: 50S ribosomal protein L2
H: 50S ribosomal protein L3
I: 50S ribosomal protein L4
J: 50S ribosomal protein L5
K: 50S ribosomal protein L6
M: 50S ribosomal protein L13
N: 50S ribosomal protein L14
O: 50S ribosomal protein L15
P: 50S ribosomal protein L16
Q: 50S ribosomal protein L17
R: 50S ribosomal protein L18
S: 50S ribosomal protein L19
T: 50S ribosomal protein L20
U: 50S ribosomal protein L21
V: 50S ribosomal protein L22
W: 50S ribosomal protein L23
X: 50S ribosomal protein L24
Y: 50S ribosomal protein L27
Z: 50S ribosomal protein L28
a: 16S rRNA
c: 30S ribosomal protein S2
d: 30S ribosomal protein S3
e: 30S ribosomal protein S4
f: 30S ribosomal protein S5
g: 30S ribosomal protein S6
h: 30S ribosomal protein S7
i: 30S ribosomal protein S8
j: 30S ribosomal protein S9
k: 30S ribosomal protein S10
l: 30S ribosomal protein S11
m: 30S ribosomal protein S12
n: 30S ribosomal protein S13
o: 30S ribosomal protein S14 type Z
p: 30S ribosomal protein S15
q: 30S ribosomal protein S16
r: 30S ribosomal protein S17
s: 30S ribosomal protein S18
t: 30S ribosomal protein S19
u: 30S ribosomal protein S20
D: tRNA-fMETi
b: RNA (5'-R(P*GP*GP*AP*GP*GP*UP*AP*UP*GP*AP*CP*AP*A)-3')
F: 50S ribosomal protein L1
3: 50S ribosomal protein L31 type B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)2,232,137238
Polymers2,225,86753
Non-polymers6,270185
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: Map and tRNA microarray indicate that 70S ribosome is initiating.
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 1 types, 1 molecules 0

#1: Protein ABC-F type ribosomal protection protein Lsa(A)


Mass: 62372.363 Da / Num. of mol.: 1 / Mutation: E142Q, E452Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Enterococcus faecalis (bacteria) / Gene: DVW78_08325 / Production host: Enterococcus faecalis (bacteria) / Strain (production host): TX5332 / References: UniProt: A0A4U4C430

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50S ribosomal protein ... , 28 types, 28 molecules 1245678GHIJKMNOPQRSTUVWXYZF3

#2: Protein 50S ribosomal protein L29


Mass: 7342.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKV0
#3: Protein 50S ribosomal protein L30


Mass: 6365.469 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKW1
#4: Protein 50S ribosomal protein L32


Mass: 6548.759 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XMM2
#5: Protein/peptide 50S ribosomal protein L33


Mass: 6052.027 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XR98
#6: Protein/peptide 50S ribosomal protein L34


Mass: 5373.507 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XSI4
#7: Protein 50S ribosomal protein L35


Mass: 7727.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XM73
#8: Protein/peptide 50S ribosomal protein L36


Mass: 4440.534 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKT9
#11: Protein 50S ribosomal protein L2


Mass: 30291.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKR6
#12: Protein 50S ribosomal protein L3


Mass: 22758.479 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKR3
#13: Protein 50S ribosomal protein L4


Mass: 22549.717 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A4U4BZI1
#14: Protein 50S ribosomal protein L5


Mass: 20123.490 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS2
#15: Protein 50S ribosomal protein L6


Mass: 19437.303 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A4U4BXV7
#16: Protein 50S ribosomal protein L13


Mass: 16325.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XSB2
#17: Protein 50S ribosomal protein L14


Mass: 13165.275 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS1
#18: Protein 50S ribosomal protein L15


Mass: 15602.868 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKT1
#19: Protein 50S ribosomal protein L16


Mass: 16261.168 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKU1
#20: Protein 50S ribosomal protein L17


Mass: 14503.704 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKX1
#21: Protein 50S ribosomal protein L18


Mass: 12937.829 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS7
#22: Protein 50S ribosomal protein L19


Mass: 13244.479 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XPL8
#23: Protein 50S ribosomal protein L20


Mass: 13674.152 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XM76
#24: Protein 50S ribosomal protein L21


Mass: 11166.986 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XMC1
#25: Protein 50S ribosomal protein L22


Mass: 12473.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKT6
#26: Protein 50S ribosomal protein L23


Mass: 11089.021 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKR7
#27: Protein 50S ribosomal protein L24


Mass: 11137.063 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKV5
#28: Protein 50S ribosomal protein L27


Mass: 10175.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XMB1
#29: Protein 50S ribosomal protein L28


Mass: 7005.314 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XRZ8
#52: Protein 50S ribosomal protein L1


Mass: 24495.230 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XR48
#53: Protein 50S ribosomal protein L31 type B


Mass: 10138.101 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XMV6

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RNA chain , 5 types, 5 molecules ABaDb

#9: RNA chain 23S rRNA


Mass: 944000.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria)
#10: RNA chain 5S rRNA


Mass: 37433.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria)
#30: RNA chain 16S rRNA


Mass: 504170.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria)
#50: RNA chain tRNA-fMETi


Mass: 24811.795 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria)
#51: RNA chain RNA (5'-R(P*GP*GP*AP*GP*GP*UP*AP*UP*GP*AP*CP*AP*A)-3')


Mass: 5617.279 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria)

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30S ribosomal protein ... , 19 types, 19 molecules cdefghijklmnopqrstu

#31: Protein 30S ribosomal protein S2


Mass: 29500.635 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XQD8
#32: Protein 30S ribosomal protein S3


Mass: 24415.184 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKR8
#33: Protein 30S ribosomal protein S4


Mass: 23273.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XRV7
#34: Protein 30S ribosomal protein S5


Mass: 17444.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKW0
#35: Protein 30S ribosomal protein S6


Mass: 11621.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKB6
#36: Protein 30S ribosomal protein S7


Mass: 17864.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKQ3
#37: Protein 30S ribosomal protein S8


Mass: 14936.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS6
#38: Protein 30S ribosomal protein S9


Mass: 14271.480 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XSA2
#39: Protein 30S ribosomal protein S10


Mass: 11731.739 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKR5
#40: Protein 30S ribosomal protein S11


Mass: 13739.913 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKV1
#41: Protein 30S ribosomal protein S12


Mass: 15309.817 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKQ7
#42: Protein 30S ribosomal protein S13


Mass: 13595.774 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKT7
#43: Protein 30S ribosomal protein S14 type Z


Mass: 7172.593 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKT0
#44: Protein 30S ribosomal protein S15


Mass: 10668.236 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XRW3
#45: Protein 30S ribosomal protein S16


Mass: 10356.150 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XP69
#46: Protein 30S ribosomal protein S17


Mass: 10332.100 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS3
#47: Protein 30S ribosomal protein S18


Mass: 9262.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKB3
#48: Protein 30S ribosomal protein S19


Mass: 10586.332 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XKS0
#49: Protein 30S ribosomal protein S20


Mass: 8972.320 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Enterococcus faecalis (bacteria) / References: UniProt: A0A1B4XQJ7

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Non-polymers , 5 types, 185 molecules

#54: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#55: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 147 / Source method: obtained synthetically / Formula: Mg
#56: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#57: Chemical...
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: K
#58: Chemical
ChemComp-PUT / 1,4-DIAMINOBUTANE / PUTRESCINE


Mass: 88.151 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H12N2

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: LsaA-in complex with 70S ribosome, mRNA, and tRNA / Type: RIBOSOME / Entity ID: #1-#53 / Source: NATURAL
Molecular weightValue: 2.2 MDa / Experimental value: NO
Source (natural)Organism: Enterococcus faecalis (bacteria)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K / Details: 5s blotting

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: -2200 nm / Nominal defocus min: -700 nm / Cs: 2.7 mm
Image recordingElectron dose: 38 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1

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Processing

EM software
IDNameVersionCategory
4CTFFIND4CTF correction
11RELIONfinal Euler assignment
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 59262 / Symmetry type: POINT

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