3EB8

VirA

Summary for 3EB8

• Entry DOI: 10.2210/pdb3eb8/pdb
• Descriptor: Cysteine protease-like virA (2 entities in total)
• Functional Keywords: beta sheet, alpha helix, hydrolase, protease, secreted, thiol protease, virulence
• Biological source: Shigella flexneri
• Total number of polymer chains: 2
• Total formula weight: 79745.83

Authors

Germane, K.L.,Spiller, B.W. (deposition date: 2008-08-27, release date: 2008-09-30, Last modification date: 2024-02-21)

Primary citation

Germane, K.L.,Ohi, R.,Goldberg, M.B.,Spiller, B.W.
Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules.
Biochemistry, 47:10241-10243, 2008

PubMed Abstract: VirA, an essential virulence factor in Shigella disease pathogenesis, is involved in the uptake, motility, and cell-to-cell spread of Shigella organisms within the human host. These functions have been attributed to a VirA protease activity and a mechanism of microtubule destruction via tubulin degradation [Yoshida, S., et al. (2006) Science 314, 985-989]. We report functional and crystallographic data indicating a novel VirA structure that lacks these activities but highlights the homology to the EspG virulence factor of pathogenic Escherichia coli.

PubMed: 18763811
DOI: 10.1021/bi801533k

Experimental method

X-RAY DIFFRACTION (2.4 Å)