Proteopedia

3h7x

A transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled coil segment of trimeric autotransporter adhesins - the wildtype structureA transition from strong right-handed to canonical left-handed supercoiling in a conserved coiled coil segment of trimeric autotransporter adhesins - the wildtype structure

Structural highlights

3h7x is a 6 chain structure with sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

YADA2_YEREN Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance.[1] [2]

See Also

References

  1. ↑ Roggenkamp A, Ackermann N, Jacobi CA, Truelzsch K, Hoffmann H, Heesemann J. Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA. J Bacteriol. 2003 Jul;185(13):3735-44. PMID:12813066
  2. ↑ Emody L, Heesemann J, Wolf-Watz H, Skurnik M, Kapperud G, O'Toole P, Wadstrom T. Binding to collagen by Yersinia enterocolitica and Yersinia pseudotuberculosis: evidence for yopA-mediated and chromosomally encoded mechanisms. J Bacteriol. 1989 Dec;171(12):6674-9. PMID:2592347

3h7x, resolution 2.00Å

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OCA
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