5FQ6

Crystal structure of the SusCD complex BT2261-2264 from Bacteroides thetaiotaomicron


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.201 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Structural basis for nutrient acquisition by dominant members of the human gut microbiota.

Glenwright, A.J.Pothula, K.R.Bhamidimarri, S.P.Chorev, D.S.Basle, A.Firbank, S.J.Zheng, H.Robinson, C.V.Winterhalter, M.Kleinekathofer, U.Bolam, D.N.van den Berg, B.

(2017) Nature 541: 407-411

  • DOI: https://doi.org/10.1038/nature20828
  • Primary Citation of Related Structures:  
    5FQ3, 5FQ4, 5FQ6, 5FQ7, 5FQ8, 5LX8, 5T3R, 5T4Y

  • PubMed Abstract: 

    The human large intestine is populated by a high density of microorganisms, collectively termed the colonic microbiota, which has an important role in human health and nutrition. The survival of microbiota members from the dominant Gram-negative phylum Bacteroidetes depends on their ability to degrade dietary glycans that cannot be metabolized by the host. The genes encoding proteins involved in the degradation of specific glycans are organized into co-regulated polysaccharide utilization loci, with the archetypal locus sus (for starch utilisation system) encoding seven proteins, SusA-SusG. Glycan degradation mainly occurs intracellularly and depends on the import of oligosaccharides by an outer membrane protein complex composed of an extracellular SusD-like lipoprotein and an integral membrane SusC-like TonB-dependent transporter. The presence of the partner SusD-like lipoprotein is the major feature that distinguishes SusC-like proteins from previously characterized TonB-dependent transporters. Many sequenced gut Bacteroides spp. encode over 100 SusCD pairs, of which the majority have unknown functions and substrate specificities. The mechanism by which extracellular substrate binding by SusD proteins is coupled to outer membrane passage through their cognate SusC transporter is unknown. Here we present X-ray crystal structures of two functionally distinct SusCD complexes purified from Bacteroides thetaiotaomicron and derive a general model for substrate translocation. The SusC transporters form homodimers, with each β-barrel protomer tightly capped by SusD. Ligands are bound at the SusC-SusD interface in a large solvent-excluded cavity. Molecular dynamics simulations and single-channel electrophysiology reveal a 'pedal bin' mechanism, in which SusD moves away from SusC in a hinge-like fashion in the absence of ligand to expose the substrate-binding site to the extracellular milieu. These data provide mechanistic insights into outer membrane nutrient import by members of the microbiota, an area of major importance for understanding human-microbiota symbiosis.


  • Organizational Affiliation

    Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PUTATIVE LIPOPROTEIN
A, C, H, L
480Bacteroides thetaiotaomicronMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q8A5H6 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
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Go to UniProtKB:  Q8A5H6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8A5H6
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
SUSC/RAGA FAMILY TONB-LINKED OUTER MEMBRANE PROTEIN
B, D, I, M
984Bacteroides thetaiotaomicronMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q8A5H5 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
Explore Q8A5H5 
Go to UniProtKB:  Q8A5H5
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UniProt GroupQ8A5H5
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
UNCHARACTERIZED PROTEIN
E, F, J, N
148Bacteroides thetaiotaomicronMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for Q8A5H8 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50))
Explore Q8A5H8 
Go to UniProtKB:  Q8A5H8
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UniProt GroupQ8A5H8
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  • Reference Sequence

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
BT_2261
G, K, O, P
10Bacteroides thetaiotaomicronMutation(s): 0 
Entity Groups  
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
KR0
Query on KR0

Download Ideal Coordinates CCD File 
Q [auth B],
T [auth D],
W [auth I],
Z [auth M]
3-decanoyloxypropyl decanoate
C23 H44 O4
PXVAQENAIBBOHT-UHFFFAOYSA-N
CA
Query on CA

Download Ideal Coordinates CCD File 
BA [auth M],
S [auth B],
V [auth D],
Y [auth I]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
NA
Query on NA

Download Ideal Coordinates CCD File 
AA [auth M],
R [auth B],
U [auth D],
X [auth I]
SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.255 
  • R-Value Work: 0.198 
  • R-Value Observed: 0.201 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 222.027α = 90
b = 91.941β = 98.23
c = 261.219γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-12-21
    Type: Initial release
  • Version 1.1: 2017-01-18
    Changes: Database references
  • Version 1.2: 2017-01-25
    Changes: Database references
  • Version 1.3: 2017-02-01
    Changes: Database references
  • Version 1.4: 2024-01-10
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description