6TXT

Major subunit ComGC from S. sanguinis Com pseudopili


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The major subunit of widespread competence pili exhibits a novel and conserved type IV pilin fold.

Sheppard, D.Berry, J.L.Denise, R.Rocha, E.P.C.Matthews, S.Pelicic, V.

(2020) J Biol Chem 295: 6594-6604

  • DOI: https://doi.org/10.1074/jbc.RA120.013316
  • Primary Citation of Related Structures:  
    6TXT, 6Y1H

  • PubMed Abstract: 

    Type IV filaments (T4F), which are helical assemblies of type IV pilins, constitute a superfamily of filamentous nanomachines virtually ubiquitous in prokaryotes that mediate a wide variety of functions. The competence (Com) pilus is a widespread T4F, mediating DNA uptake (the first step in natural transformation) in bacteria with one membrane (monoderms), an important mechanism of horizontal gene transfer. Here, we report the results of genomic, phylogenetic, and structural analyses of ComGC, the major pilin subunit of Com pili. By performing a global comparative analysis, we show that Com pili genes are virtually ubiquitous in Bacilli, a major monoderm class of Firmicutes. This also revealed that ComGC displays extensive sequence conservation, defining a monophyletic group among type IV pilins. We further report ComGC solution structures from two naturally competent human pathogens, Streptococcus sanguinis (ComGC SS ) and Streptococcus pneumoniae (ComGC SP ), revealing that this pilin displays extensive structural conservation. Strikingly, ComGC SS and ComGC SP exhibit a novel type IV pilin fold that is purely helical. Results from homology modeling analyses suggest that the unusual structure of ComGC is compatible with helical filament assembly. Because ComGC displays such a widespread distribution, these results have implications for hundreds of monoderm species.


  • Organizational Affiliation

    Medical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Competence pilin-like protein ComGC72Streptococcus sanguinisMutation(s): 0 
Gene Names: comGCSSV_0099
UniProt
Find proteins for A0A0B7GIC8 (Streptococcus sanguinis)
Explore A0A0B7GIC8 
Go to UniProtKB:  A0A0B7GIC8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0B7GIC8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (MRC, United Kingdom)United KingdomMR/P022197/1

Revision History  (Full details and data files)

  • Version 1.0: 2020-04-15
    Type: Initial release
  • Version 1.1: 2020-04-22
    Changes: Database references
  • Version 1.2: 2020-05-20
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Database references, Other