2cc3: Difference between revisions
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Revision as of 18:59, 5 November 2007
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STRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEIN
OverviewOverview
Bacterial type IV secretion systems (T4SS) translocate DNA and/or proteins, to recipient cells, thus providing a mechanism for conjugative transfer of, genetic material and bacterial pathogenesis. Here we describe the first, structure of a core component from the archetypal Agrobacterium, tumefaciens T4SS: the 2.2-A resolution crystal structure of the VirB8, periplasmic domain (pVirB8(AT)). VirB8 forms a dimer in the crystal, and, we identify residues likely important for stabilization of the dimer, interface. Structural comparison of pVirB8(AT) with Brucella suis VirB8, confirms that the monomers have a similar fold. In addition, the, pVirB8(AT) dimer superimposes very closely on the B. suis VirB8 dimer, supporting the proposal that dimer formation in the crystal reflects, self-interactions that are biologically significant. The evolutionary, conservation level for each residue was obtained from a data set of 84, VirB8 homologs and projected onto the protein structure to indicate, conserved surface patches that likely contact other T4SS proteins.
About this StructureAbout this Structure
2CC3 is a Single protein structure of sequence from Agrobacterium tumefaciens with MPD as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites., Bailey S, Ward D, Middleton R, Grossmann JG, Zambryski PC, Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2582-7. Epub 2006 Feb 15. PMID:16481621
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