2cc3: Difference between revisions

Revision as of 20:43, 27 July 2008

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File:2cc3.png

Template:STRUCTURE 2cc3

STRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEINSTRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEIN

Template:ABSTRACT PUBMED 16481621

About this StructureAbout this Structure

2CC3 is a Single protein structure of sequence from Agrobacterium tumefaciens. 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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-'''STRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEIN'''
+===STRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEIN===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16481621}}, adds the Publication Abstract to the page
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 [[Category: Type iv secretion system]]
 [[Category: Virb8]]
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