7BGL

Salmonella LP ring 26 mer refined in C26 map


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 2.2 of the entry. See complete history


Literature

Molecular structure of the intact bacterial flagellar basal body.

Johnson, S.Furlong, E.J.Deme, J.C.Nord, A.L.Caesar, J.J.E.Chevance, F.F.V.Berry, R.M.Hughes, K.T.Lea, S.M.

(2021) Nat Microbiol 6: 712-721

  • DOI: https://doi.org/10.1038/s41564-021-00895-y
  • Primary Citation of Related Structures:  
    7BGL, 7BHQ, 7BIN, 7BJ2, 7BK0, 7NVG

  • PubMed Abstract: 

    The bacterial flagellum is a macromolecular protein complex that enables motility in many species. Bacterial flagella self-assemble a strong, multicomponent drive shaft that couples rotation in the inner membrane to the micrometre-long flagellar filament that powers bacterial swimming in viscous fluids 1-3 . Here, we present structures of the intact Salmonella flagellar basal body 4 , encompassing the inner membrane rotor, drive shaft and outer-membrane bushing, solved using cryo-electron microscopy to resolutions of 2.2-3.7 Å. The structures reveal molecular details of how 173 protein molecules of 13 different types assemble into a complex spanning two membranes and a cell wall. The helical drive shaft at one end is intricately interwoven with the rotor component with both the export gate complex and the proximal rod forming interactions with the MS-ring. At the other end, the drive shaft distal rod passes through the LP-ring bushing complex, which functions as a molecular bearing anchored in the outer membrane through interactions with the lipopolysaccharide. The in situ structure of a protein complex capping the drive shaft provides molecular insights into the assembly process of this molecular machine.


  • Organizational Affiliation

    Sir William Dunn School of Pathology, University of Oxford, Oxford, UK. steven.johnson@path.ox.ac.uk.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Flagellar L-ring protein232Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P0A1N8 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P0A1N8 
Go to UniProtKB:  P0A1N8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A1N8
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Flagellar P-ring protein365Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P15930 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P15930 
Go to UniProtKB:  P15930
Entity Groups  
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UniProt GroupP15930
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
YecR111Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for A0A745A2I3 (Salmonella typhi)
Explore A0A745A2I3 
Go to UniProtKB:  A0A745A2I3
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A745A2I3
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
TQN
Query on TQN

Download Ideal Coordinates CCD File 
BC [auth A]
BD [auth N]
DC [auth B]
DD [auth O]
FC [auth C]
BC [auth A],
BD [auth N],
DC [auth B],
DD [auth O],
FC [auth C],
FD [auth P],
HC [auth D],
HD [auth Q],
JC [auth E],
JD [auth R],
LC [auth F],
LD [auth S],
NC [auth G],
ND [auth T],
PC [auth H],
PD [auth U],
RC [auth I],
RD [auth V],
TC [auth J],
TD [auth W],
VC [auth K],
VD [auth X],
XC [auth L],
XD [auth Y],
ZC [auth M],
ZD [auth Z]
[(3~{R})-1-[[(2~{R},3~{R},4~{R},5~{S},6~{R})-6-[[(2~{R},3~{R},4~{R},5~{S},6~{R})-3-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-(hydroxymethyl)-5-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]oxymethyl]-5-oxidanyl-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-2-phosphonooxy-oxan-3-yl]amino]-1-oxidanylidene-tetradecan-3-yl] hexadecanoate
C110 H208 N2 O26 P2
VOXDTCSXQHOYKC-XGEOUJBZSA-N
TLW
Query on TLW

Download Ideal Coordinates CCD File 
AC [auth A]
AD [auth M]
CC [auth A]
CD [auth N]
EC [auth B]
AC [auth A],
AD [auth M],
CC [auth A],
CD [auth N],
EC [auth B],
ED [auth O],
GC [auth C],
GD [auth P],
IC [auth D],
ID [auth Q],
KC [auth E],
KD [auth R],
MC [auth F],
MD [auth S],
OC [auth G],
OD [auth T],
QC [auth H],
QD [auth U],
SC [auth I],
SD [auth V],
UC [auth J],
UD [auth W],
WC [auth K],
WD [auth X],
YC [auth L],
YD [auth Y]
(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-4,5-bis(oxidanyl)oxane-2-carboxylic acid
C8 H14 O7
ANWKOKWAJKGXFO-NYMZXIIRSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 2.20 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION3.1

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Wellcome TrustUnited Kingdom219477
Wellcome TrustUnited Kingdom209194
Wellcome TrustUnited Kingdom201536
Medical Research Council (MRC, United Kingdom)United KingdomS021264

Revision History  (Full details and data files)

  • Version 1.0: 2021-05-05
    Type: Initial release
  • Version 2.0: 2021-05-19
    Changes: Database references, Non-polymer description
  • Version 2.1: 2021-06-09
    Changes: Database references
  • Version 2.2: 2021-07-14
    Changes: Derived calculations