7TTC | pdb_00007ttc

BamABCDE bound to substrate EspP


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.60 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.

Doyle, M.T.Jimah, J.R.Dowdy, T.Ohlemacher, S.I.Larion, M.Hinshaw, J.E.Bernstein, H.D.

(2022) Cell 185: 1143

  • DOI: https://doi.org/10.1016/j.cell.2022.02.016
  • Primary Citation of Related Structures:  
    7TSZ, 7TT0, 7TT1, 7TT2, 7TT3, 7TT4, 7TT5, 7TT6, 7TT7, 7TTC

  • PubMed Abstract: 

    Transmembrane β barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the β barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. Here, we used single-particle cryo-EM to visualize the folding dynamics of a model β barrel protein (EspP) by BAM. We found that BAM binds the highly conserved "β signal" motif of EspP to correctly orient β strands in the OM during folding. We also found that the folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated β sheets are attached to the essential BAM subunit, BamA. The structures show an unprecedented deflection of the membrane surrounding the EspP intermediates and suggest that β sheets progressively fold toward BamA to form a β barrel. Along with in vivo experiments that tracked β barrel folding while the OM tension was modified, our results support a model in which BAM harnesses OM elasticity to accelerate β barrel folding.


  • Organizational Affiliation

    Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Outer membrane protein assembly factor BamBA [auth B]373Escherichia coliMutation(s): 0 
Gene Names: bamByfgLb2512JW2496
Membrane Entity: Yes 
UniProt
Find proteins for P77774 (Escherichia coli (strain K12))
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Go to UniProtKB:  P77774
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UniProt GroupP77774
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Outer membrane protein assembly factor BamAB [auth A]800Escherichia coliMutation(s): 0 
Gene Names: 
Membrane Entity: Yes 
UniProt
Find proteins for P0A940 (Escherichia coli (strain K12))
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Go to UniProtKB:  P0A940
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UniProt GroupP0A940
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Outer membrane protein assembly factor BamEC [auth E]94Escherichia coliMutation(s): 0 
Gene Names: 
Membrane Entity: Yes 
UniProt
Find proteins for P0A937 (Escherichia coli (strain K12))
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Go to UniProtKB:  P0A937
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UniProt GroupP0A937
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Outer membrane protein assembly factor BamD226Escherichia coliMutation(s): 0 
Gene Names: bamDEAMG_00990
Membrane Entity: Yes 
UniProt
Find proteins for P0AC02 (Escherichia coli (strain K12))
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UniProt GroupP0AC02
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Outer membrane protein assembly factor BamCE [auth C]320Escherichia coliMutation(s): 0 
Gene Names: 
Membrane Entity: Yes 
UniProt
Find proteins for P0A903 (Escherichia coli (strain K12))
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UniProt GroupP0A903
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Serine protease EspPF [auth P]277Escherichia coliMutation(s): 0 
Gene Names: espPL7020ECO57PM78
EC: 3.4.21
Membrane Entity: Yes 
UniProt
Find proteins for O32591 (Escherichia coli)
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UniProt GroupO32591
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Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
K33 (Subject of Investigation/LOI)
Query on K33

Download Ideal Coordinates CCD File 
G [auth A]2,3-dideoxy-6-O-[2-deoxy-4-O-phosphono-2-(tetradecanoylamino)-alpha-L-gulopyranosyl]-1-O-phosphono-beta-D-threo-hexopyranose
C26 H51 N O15 P2
RLOUQIAPEYIPKB-RYYOIEMHSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.60 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)United States1ZIADK052037
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)United States1ZIADK060100

Revision History  (Full details and data files)

  • Version 1.0: 2022-03-30
    Type: Initial release
  • Version 1.1: 2022-04-13
    Changes: Database references
  • Version 1.2: 2024-11-06
    Changes: Data collection, Structure summary