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- PDB-2zjq: Interaction of L7 with L11 induced by Microccocin binding to the ... -

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Basic information

Entry
Database: PDB / ID: 2zjq
TitleInteraction of L7 with L11 induced by Microccocin binding to the Deinococcus radiodurans 50S subunit
Components
  • (50S ribosomal protein ...) x 29
  • ribosomal 23S RNA
  • ribosomal 5S RNA
KeywordsRIBOSOME / ribosomal subunit / 50S / thiopeptide antibiotics / complex / translational regulation / L11 / molecular switch / L7 / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / tRNA-binding / Methylation / Metal-binding / Zinc-finger
Function / homology
Function and homology information


ribosome assembly / large ribosomal subunit rRNA binding / cytoplasmic translation / cytosolic large ribosomal subunit / large ribosomal subunit / ribosomal large subunit assembly / 5S rRNA binding / transferase activity / negative regulation of translation / tRNA binding ...ribosome assembly / large ribosomal subunit rRNA binding / cytoplasmic translation / cytosolic large ribosomal subunit / large ribosomal subunit / ribosomal large subunit assembly / 5S rRNA binding / transferase activity / negative regulation of translation / tRNA binding / ribosome / rRNA binding / structural constituent of ribosome / translation / mRNA binding / RNA binding / metal ion binding
Similarity search - Function
Ribosomal protein L25, C-terminal domain / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12, N-terminal domain / Ribosomal protein L17 / 50s Ribosomal Protein L17; Chain: A, / Ribosomal Protein L25; Chain P / Ribosomal protein L13 / Ribosomal Protein L13p; Chain: A; / Ribosomal protein L11/L12, C-terminal domain / Ribosomal protein L6 ...Ribosomal protein L25, C-terminal domain / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12, N-terminal domain / Ribosomal protein L17 / 50s Ribosomal Protein L17; Chain: A, / Ribosomal Protein L25; Chain P / Ribosomal protein L13 / Ribosomal Protein L13p; Chain: A; / Ribosomal protein L11/L12, C-terminal domain / Ribosomal protein L6 / Ribosomal Protein L25; Chain P / 50s Ribosomal Protein L5; Chain: A, / Ribosomal protein L5 / Ribosomal protein L30/L7 / Nucleotidyltransferase; domain 5 - #100 / Ribosomal protein L16/L10 / Ribosomal protein L7/L12, oligomerisation / Ribosomal protein L22/L17 / Ribosomal protein L7/L12 dimerisation domain / Ribosomal protein L7/L12, oligomerisation domain superfamily / Ribosomal protein L7/L12 / Ribosomal protein L7/L12, C-terminal / Ribosomal protein L7/L12 C-terminal domain / Ribosomal protein L14/L23 / Ribosomal Protein L14 / Outer Surface Protein A; domain 3 / Ribosomal protein L7/L12, C-terminal/adaptor protein ClpS-like / Ribosomal Protein L22; Chain A / Ribosomal Protein L30; Chain: A, / Aldehyde Oxidoreductase; domain 3 / RNA Polymerase Alpha Subunit; Chain A, domain 2 / Ribosomal protein L25, long-form / Ribosomal protein TL5, C-terminal domain / Ribosomal protein L25, beta domain / Ribosomal protein L25, C-terminal / RRM (RNA recognition motif) domain / Ribosomal protein L11, bacterial-type / Ribosomal protein L11 signature. / Ribosomal protein L11, conserved site / Ribosomal protein L16 signature 1. / Ribosomal protein L16 signature 2. / Ribosomal protein L16, conserved site / Ribosomal protein L17 signature. / Ribosomal protein L28/L24 superfamily / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11, N-terminal / Ribosomal protein L32p, bacterial type / Ribosomal protein L11/L12 / Ribosomal protein L11, RNA binding domain / Ribosomal protein L11, C-terminal / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L36 signature. / Ribosomal L25p family / Ribosomal protein L25 / Ribosomal protein L28 / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35 signature. / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L35, conserved site / Ribosomal protein L25/Gln-tRNA synthetase, N-terminal / Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain superfamily / Nucleic acid-binding proteins / Ribosomal protein L5, bacterial-type / Ribosomal protein L18, bacterial-type / Ribosomal protein L34 signature. / Ribosomal protein L34, conserved site / Ribosomal protein L19 signature. / Ribosomal protein L19, conserved site / Ribosomal protein L6, bacterial-type / Ribosomal protein L20 signature. / Ribosomal protein L27 signature. / Ribosomal protein L27, conserved site / Ribosomal protein L36 / Ribosomal protein L36 / Ribosomal protein L36 superfamily / Ribosomal protein L14P, bacterial-type / Ribosomal protein L2, bacterial/organellar-type / Ribosomal L28 family / Ribosomal protein L35 superfamily / Ribosomal protein L35 / Ribosomal protein L33 / Ribosomal protein L35 / Ribosomal protein L28/L24 / Ribosomal protein L33 / Ribosomal protein L33 superfamily / Ribosomal protein L18 / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / L28p-like / Ribosomal protein L16 / Ribosomal protein L20 / Ribosomal L32p protein family / Ribosomal protein L20 / Ribosomal protein L20, C-terminal / Ribosomal protein L30, bacterial-type / Ribosomal protein L34 / Ribosomal proteins 50S L24/mitochondrial 39S L24 / Ribosomal protein L34
Similarity search - Domain/homology
RNA (> 1000) / 50S ribosomal protein L16 / 50S ribosomal protein L25 / 50S ribosomal protein L5 / 50S ribosomal protein L24 / 50S ribosomal protein L14 / 50S ribosomal protein L29 / 50S ribosomal protein L2 / 50S ribosomal protein L22 / 50S ribosomal protein L20 ...RNA (> 1000) / 50S ribosomal protein L16 / 50S ribosomal protein L25 / 50S ribosomal protein L5 / 50S ribosomal protein L24 / 50S ribosomal protein L14 / 50S ribosomal protein L29 / 50S ribosomal protein L2 / 50S ribosomal protein L22 / 50S ribosomal protein L20 / 50S ribosomal protein L23 / 50S ribosomal protein L4 / 50S ribosomal protein L3 / 50S ribosomal protein L13 / 50S ribosomal protein L21 / 50S ribosomal protein L19 / 50S ribosomal protein L35 / RNA (> 100) / 50S ribosomal protein L7/L12 / 50S ribosomal protein L11 / 50S ribosomal protein L33 / 50S ribosomal protein L6 / 50S ribosomal protein L18 / 50S ribosomal protein L30 / 50S ribosomal protein L15 / 50S ribosomal protein L36 / 50S ribosomal protein L17 / 50S ribosomal protein L34 / 50S ribosomal protein L28 / 50S ribosomal protein L32 / RNA / RNA (> 10) / 50S ribosomal protein L27
Similarity search - Component
Biological speciesDeinococcus radiodurans (radioresistant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsHarms, J.M. / Wilson, D.N. / Schluenzen, F. / Connell, S.R. / Stachelhaus, T. / Zaborowska, Z. / Spahn, C.M.T. / Fucini, P.
CitationJournal: Mol.Cell / Year: 2008
Title: Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.
Authors: Harms, J.M. / Wilson, D.N. / Schluenzen, F. / Connell, S.R. / Stachelhaus, T. / Zaborowska, Z. / Spahn, C.M. / Fucini, P.
History
DepositionMar 8, 2008Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 17, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 16, 2014Group: Refinement description

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
X: ribosomal 23S RNA
Y: ribosomal 5S RNA
A: 50S ribosomal protein L2
B: 50S ribosomal protein L3
C: 50S ribosomal protein L4
D: 50S ribosomal protein L5
E: 50S ribosomal protein L6
F: 50S ribosomal protein L11
G: 50S ribosomal protein L13
H: 50S ribosomal protein L14
I: 50S ribosomal protein L15
J: 50S ribosomal protein L16
K: 50S ribosomal protein L17
L: 50S ribosomal protein L18
M: 50S ribosomal protein L19
N: 50S ribosomal protein L20
O: 50S ribosomal protein L21
P: 50S ribosomal protein L22
Q: 50S ribosomal protein L23
R: 50S ribosomal protein L24
S: 50S ribosomal protein L25
T: 50S ribosomal protein L27
U: 50S ribosomal protein L28
V: 50S ribosomal protein L29
W: 50S ribosomal protein L30
Z: 50S ribosomal protein L32
1: 50S ribosomal protein L33
2: 50S ribosomal protein L34
3: 50S ribosomal protein L35
4: 50S ribosomal protein L36
5: 50S ribosomal protein L7/L12


Theoretical massNumber of molelcules
Total (without water)1,376,75231
Polymers1,376,75231
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)169.900, 408.900, 694.500
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

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RNA chain , 2 types, 2 molecules XY

#1: RNA chain ribosomal 23S RNA


Mass: 933405.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant)
#2: RNA chain ribosomal 5S RNA


Mass: 39276.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant)

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50S ribosomal protein ... , 29 types, 29 molecules ABCDEFGHIJKLMNOPQRSTUVWZ12345

#3: Protein 50S ribosomal protein L2 /


Mass: 29976.580 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ9
#4: Protein 50S ribosomal protein L3 /


Mass: 22477.150 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXK2
#5: Protein 50S ribosomal protein L4 /


Mass: 22308.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXK1
#6: Protein 50S ribosomal protein L5 /


Mass: 20379.908 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ0
#7: Protein 50S ribosomal protein L6 /


Mass: 19613.637 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSL3
#8: Protein 50S ribosomal protein L11 /


Mass: 14889.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSS7
#9: Protein 50S ribosomal protein L13 /


Mass: 19223.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXY1
#10: Protein 50S ribosomal protein L14 /


Mass: 14256.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ2
#11: Protein 50S ribosomal protein L15 /


Mass: 16894.184 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSK9
#12: Protein 50S ribosomal protein L16 /


Mass: 16257.194 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ5
#13: Protein 50S ribosomal protein L17 /


Mass: 12926.067 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSJ5
#14: Protein 50S ribosomal protein L18 /


Mass: 12163.936 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSL2
#15: Protein 50S ribosomal protein L19 /


Mass: 18347.818 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RWB4
#16: Protein 50S ribosomal protein L20 /


Mass: 13991.274 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSW7
#17: Protein 50S ribosomal protein L21 /


Mass: 11165.743 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RY64
#18: Protein 50S ribosomal protein L22 /


Mass: 15190.869 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ7
#19: Protein 50S ribosomal protein L23 /


Mass: 10539.210 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXK0
#20: Protein 50S ribosomal protein L24 /


Mass: 12384.402 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ1
#21: Protein 50S ribosomal protein L25 / / General stress protein CTC


Mass: 25415.418 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RX88
#22: Protein 50S ribosomal protein L27 /


Mass: 9609.091 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RY65
#23: Protein 50S ribosomal protein L28 /


Mass: 8982.592 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RRG8
#24: Protein 50S ribosomal protein L29 /


Mass: 7774.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RXJ4
#25: Protein 50S ribosomal protein L30 /


Mass: 6079.235 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSL0
#26: Protein 50S ribosomal protein L32 /


Mass: 6810.017 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: P49228
#27: Protein 50S ribosomal protein L33 / / Coordinate model: Cα atoms only


Mass: 6374.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSS4
#28: Protein/peptide 50S ribosomal protein L34 / / Coordinate model: Cα atoms only


Mass: 5626.587 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSH2
#29: Protein 50S ribosomal protein L35 / / Coordinate model: Cα atoms only


Mass: 7448.129 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSW6
#30: Protein/peptide 50S ribosomal protein L36 /


Mass: 4322.295 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RSK0
#31: Protein 50S ribosomal protein L7/L12 / Ribosome / Coordinate model: Cα atoms only


Mass: 12642.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Deinococcus radiodurans (radioresistant) / References: UniProt: Q9RST0

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Details

Sequence detailsTHE SEQUENCE OF THE CHAIN X (RRNA-23S) MATCHES TO RESIDUES 2587937 - 2590816 IN GENEBANK WITH ...THE SEQUENCE OF THE CHAIN X (RRNA-23S) MATCHES TO RESIDUES 2587937 - 2590816 IN GENEBANK WITH ACCESSION 11612676. THE SEQUENCE OF THE CHAIN Y (RRNA-5S) MATCHES TO RESIDUES 254392 - 254514 IN GENEBANK WITH ACCESSION 11612676.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 7

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Sample preparation

CrystalDensity Matthews: 4.38 Å3/Da / Density % sol: 71.92 %
Crystal growMethod: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONESRF ID2910.97
SYNCHROTRONSLS X06SA21
Detector
TypeIDDetectorDate
ADSC QUANTUM 3151CCD
ADSC QUANTUM 3152CCDDec 3, 2007
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.971
211
ReflectionResolution: 3.3→30 Å / Num. all: 360502 / Num. obs: 352577 / % possible obs: 97.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.133 / Net I/σ(I): 7.5
Reflection shellResolution: 3.3→3.36 Å / Mean I/σ(I) obs: 1.3 / % possible all: 89

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Processing

Software
NameClassification
HKL-2000data collection
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2ZJR

2zjr


Resolution: 3.3→30 Å / σ(F): 2 / σ(I): 2
RfactorNum. reflection% reflection
Rfree0.3386 --
obs0.3016 352577 97.8 %
all-360508 -
Refinement stepCycle: LAST / Resolution: 3.3→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24146 60249 0 0 84395
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.010592
X-RAY DIFFRACTIONc_angle_deg1.54328
LS refinement shellResolution: 3.3→3.36 Å / % reflection obs: 89 %

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