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PROSITE documentation PDOC51780

GW domain profile





Description

The GW domain or cell wall targeting (CWT) signal is a module of about 80-90 amino acids named for a conserved Gly-Trp (GW) dipeptide. GW domains have only been identified in Gram-positive bacteria and form a small protein family. They are divergent members of the SH3 family (see <PDOC50002>). However, GW domains are unlikely to mimic SH3 domains functionally, as their potential peptide-binding sites are destroyed or blocked. GW domains may constitute a motif for cell-surface anchoring in Listeria and other Gram-positive bacteria [1,2].

The GW domain is composed of seven β-strands, five of which are organized into an open barrel conformation like that of SH3 domains (see <PDB:1M9S>). The eponymous GW dipeptide, located in the fourth β-strand, is more conserved in GW domains than in SH3 domains. Both the glycine and tryptophan are buried in GW proteins, while the equivalent residues in SH3 proteins are surface accesible, perhaps explaning the greater conservation in GW proteins [2,3].

Some proteins known to contain a GW domain are listed below:

  • Listeria monocytogenes internalin B (InlB), an invasion protein associated with the bacterial surface.
  • Listeria monocytogenes autolysin, amidase (Ami), a surface protein with bacteriolytic activity.

The profile we developed covers the entire GW domain.

Last update:

November 2015 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

GW, PS51780; GW domain profile  (MATRIX)


References

1AuthorsBraun L. Dramsi S. Dehoux P. Bierne H. Lindahl G. Cossart P.
TitleInlB: an invasion protein of Listeria monocytogenes with a novel type of surface association.
SourceMol. Microbiol. 25:285-294(1997).
PubMed ID9282740

2AuthorsMarino M. Banerjee M. Jonquieres R. Cossart P. Ghosh P.
TitleGW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands.
SourceEMBO J. 21:5623-5634(2002).
PubMed ID12411480

3AuthorsZoll S. Schlag M. Shkumatov A.V. Rautenberg M. Svergun D.I. Goetz F. Stehle T.
TitleLigand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition.
SourceJ. Bacteriol. 194:3789-3802(2012).
PubMed ID22609916
DOI10.1128/JB.00331-12



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