2cc3: Difference between revisions
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==Overview== | ==Overview== | ||
Bacterial type IV secretion systems (T4SS) translocate DNA and/or proteins | 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 Structure== | ==About this Structure== | ||
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[[Category: Middleton, R.]] | [[Category: Middleton, R.]] | ||
[[Category: Ward, D.]] | [[Category: Ward, D.]] | ||
[[Category: Zambryski, P | [[Category: Zambryski, P C.]] | ||
[[Category: MPD]] | [[Category: MPD]] | ||
[[Category: agrobacterium]] | [[Category: agrobacterium]] | ||
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[[Category: virb8]] | [[Category: virb8]] | ||
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Revision as of 14:47, 21 February 2008
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STRUCTURE OF AGROBACTERIUM TUMEFACIENS VIRB8 PROTEIN
Overview
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 Structure
2CC3 is a Single protein structure of sequence from Agrobacterium tumefaciens with MPD as ligand. Known structural/functional Site: AC1. Full crystallographic information is available from OCA.
Reference
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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