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- EMDB-30327: Mycobacterium smegmatis SugABC complex -

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Basic information

Entry
Database: EMDB / ID: EMD-30327
TitleMycobacterium smegmatis SugABC complex
Map data
Sample
  • Complex: Mycobacterium smegmatis SugABC complex
    • Protein or peptide: ABC transporter, ATP-binding protein SugC
    • Protein or peptide: ABC sugar transporter, permease component
    • Protein or peptide: ABC transporter, permease protein SugB
KeywordsABC transporter / Lipoprotein / Mycobacteria / TRANSPORT PROTEIN
Function / homology
Function and homology information


carbohydrate transport / ABC-type transporter activity / ATP-binding cassette (ABC) transporter complex / transmembrane transport / ATP hydrolysis activity / ATP binding / plasma membrane
Similarity search - Function
: / MalK, OB fold domain / : / MalK OB fold domain / ABC transporter, maltose/maltodextrin import, MalK-like / : / Molybdate/tungstate binding, C-terminal / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component ...: / MalK, OB fold domain / : / MalK OB fold domain / ABC transporter, maltose/maltodextrin import, MalK-like / : / Molybdate/tungstate binding, C-terminal / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ABC transporter, ATP-binding protein SugC / ABC transporter, permease protein SugB / ABC transporter, permease protein SugA / ABC sugar transporter, permease component
Similarity search - Component
Biological speciesMycolicibacterium smegmatis MC2 155 (bacteria) / Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.41 Å
AuthorsLiu F / Liang J
Funding support China, 2 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2017YFC0840300 China
National Natural Science Foundation of China (NSFC)81520108019 China
CitationJournal: Sci Adv / Year: 2020
Title: Structural basis of trehalose recycling by the ABC transporter LpqY-SugABC.
Authors: Fengjiang Liu / Jingxi Liang / Bing Zhang / Yan Gao / Xiuna Yang / Tianyu Hu / Haitao Yang / Wenqing Xu / Luke W Guddat / Zihe Rao /
Abstract: In bacteria, adenosine 5'-triphosphate (ATP)-binding cassette (ABC) importers are essential for the uptake of nutrients including the nonreducing disaccharide trehalose, a metabolite that is crucial ...In bacteria, adenosine 5'-triphosphate (ATP)-binding cassette (ABC) importers are essential for the uptake of nutrients including the nonreducing disaccharide trehalose, a metabolite that is crucial for the survival and virulence of several human pathogens including SugABC is an ABC transporter that translocates trehalose from the periplasmic lipoprotein LpqY into the cytoplasm of mycobacteria. Here, we report four high-resolution cryo-electron microscopy structures of the mycobacterial LpqY-SugABC complex to reveal how it binds and passes trehalose through the membrane to the cytoplasm. A unique feature observed in this system is the initial mode of capture of the trehalose at the LpqY interface. Uptake is achieved by a pivotal rotation of LpqY relative to SugABC, moving from an open and accessible conformation to a clamped conformation upon trehalose binding. These findings enrich our understanding as to how ABC transporters facilitate substrate transport across the membrane in Gram-positive bacteria.
History
DepositionJun 8, 2020-
Header (metadata) releaseDec 2, 2020-
Map releaseDec 2, 2020-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.15
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.15
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7cad
  • Surface level: 0.15
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
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Supplemental images

Downloads & links

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Map

FileDownload / File: emd_30327.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 384 pix.
= 314.88 Å
0.82 Å/pix.
x 384 pix.
= 314.88 Å
0.82 Å/pix.
x 384 pix.
= 314.88 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density
Contour LevelBy AUTHOR: 0.15 / Movie #1: 0.15
Minimum - Maximum-0.7318028 - 1.0805557
Average (Standard dev.)0.00030696386 (±0.026291208)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 314.88 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.820.820.82
M x/y/z384384384
origin x/y/z0.0000.0000.000
length x/y/z314.880314.880314.880
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ360360360
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS384384384
D min/max/mean-0.7321.0810.000

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Supplemental data

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Sample components

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Entire : Mycobacterium smegmatis SugABC complex

EntireName: Mycobacterium smegmatis SugABC complex
Components
  • Complex: Mycobacterium smegmatis SugABC complex
    • Protein or peptide: ABC transporter, ATP-binding protein SugC
    • Protein or peptide: ABC sugar transporter, permease component
    • Protein or peptide: ABC transporter, permease protein SugB

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Supramolecule #1: Mycobacterium smegmatis SugABC complex

SupramoleculeName: Mycobacterium smegmatis SugABC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mycolicibacterium smegmatis MC2 155 (bacteria)

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Macromolecule #1: ABC transporter, ATP-binding protein SugC

MacromoleculeName: ABC transporter, ATP-binding protein SugC / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Strain: ATCC 700084 / mc(2)155
Molecular weightTheoretical: 43.703609 KDa
Recombinant expressionOrganism: Mycolicibacterium smegmatis MC2 155 (bacteria)
SequenceString: MAEIVLDRVT KSYPDGAGGV RAAVKEFSMT IADGEFIILV GPSGCGKSTT LNMIAGLEEI TSGELRIGGE RVNEKAPKDR DIAMVFQSY ALYPHMTVRQ NIAFPLTLAK VPKAEIAAKV EETAKILDLS ELLDRKPGQL SGGQRQRVAM GRAIVRSPKA F LMDEPLSN ...String:
MAEIVLDRVT KSYPDGAGGV RAAVKEFSMT IADGEFIILV GPSGCGKSTT LNMIAGLEEI TSGELRIGGE RVNEKAPKDR DIAMVFQSY ALYPHMTVRQ NIAFPLTLAK VPKAEIAAKV EETAKILDLS ELLDRKPGQL SGGQRQRVAM GRAIVRSPKA F LMDEPLSN LDAKLRVQMR AEISRLQDRL GTTTVYVTHD QTEAMTLGDR VVVMLAGEVQ QIGTPDELYS SPANLFVAGF IG SPAMNFF PATRTDVGVR LPFGEVTLTP HMLDLLDKQA RPENIIVGIR PEHIEDSALL DGYARIRALT FSVRADIVES LGA DKYVHF TTEGAGAESA QLAELAADSG AGTNQFIARV SADSRVRTGE QIELAIDTTK LSIFDAATGL NLTRDITPTD PTEA AGPDA G

UniProtKB: ABC transporter, ATP-binding protein SugC

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Macromolecule #2: ABC sugar transporter, permease component

MacromoleculeName: ABC sugar transporter, permease component / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Strain: ATCC 700084 / mc(2)155
Molecular weightTheoretical: 32.73925 KDa
Recombinant expressionOrganism: Mycolicibacterium smegmatis MC2 155 (bacteria)
SequenceString: MTAAVTPSAS AVASDDKKSE RRLAFWLIAP AVLLMLAVTA YPIGYAVWLS LQRYNLAEPH DTEFIGLANY VTVLTDGYWW TAFAVTLGI TVVSVAIEFA LGLALALVMH RTIFGKGAVR TAILIPYGIV TVAASYSWYY AWTPGTGYLA NLLPEGSAPL T DQLPSLAI ...String:
MTAAVTPSAS AVASDDKKSE RRLAFWLIAP AVLLMLAVTA YPIGYAVWLS LQRYNLAEPH DTEFIGLANY VTVLTDGYWW TAFAVTLGI TVVSVAIEFA LGLALALVMH RTIFGKGAVR TAILIPYGIV TVAASYSWYY AWTPGTGYLA NLLPEGSAPL T DQLPSLAI VVLAEVWKTT PFMALLLLAG LALVPQDLLN AAQVDGAGPW KRLTKVILPM IKPAILVALL FRTLDAFRIF DN IYILTGG SNDTGSVSIL GYDNLFKAFN VGLGSAISVL IFLSVAIIAF IYIKIFGAAA PGSDEEVR

UniProtKB: ABC sugar transporter, permease component

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Macromolecule #3: ABC transporter, permease protein SugB

MacromoleculeName: ABC transporter, permease protein SugB / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (bacteria)
Strain: ATCC 700084 / mc(2)155
Molecular weightTheoretical: 29.839441 KDa
Recombinant expressionOrganism: Mycolicibacterium smegmatis MC2 155 (bacteria)
SequenceString: MADRVDARRA TWWSVVNILV IVYALIPVLW ILSLSLKPTS SVKDGKLIPT EITFANYKAI FSGDAFTSAL FNSIGIGLIT TIIAVVIGG MAAYAVARLQ FPGKQLLIGV ALLIAMFPHI SLVTPIFNMW RGIGLFDTWP GLIIPYITFA LPLAIYTLSA F FREIPWDL ...String:
MADRVDARRA TWWSVVNILV IVYALIPVLW ILSLSLKPTS SVKDGKLIPT EITFANYKAI FSGDAFTSAL FNSIGIGLIT TIIAVVIGG MAAYAVARLQ FPGKQLLIGV ALLIAMFPHI SLVTPIFNMW RGIGLFDTWP GLIIPYITFA LPLAIYTLSA F FREIPWDL EKAAKMDGAT PAQAFRKVIA PLAAPGIVTA AILVFIFAWN DLLLALSLTA TQRAITAPVA IANFTGSSQF EE PTGSIAA GAMVITIPII IFVLIFQRRI VAGLTSGAVK G

UniProtKB: ABC transporter, permease protein SugB

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.41 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 197191
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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