2CC3

Structure of Agrobacterium tumefaciens VirB8 protein

Summary for 2CC3

• Entry DOI: 10.2210/pdb2cc3/pdb
• Descriptor: PROTEIN VIRB8, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• Functional Keywords: secretion system, virb8, agrobacterium, type iv secretion system, consurf
• Biological source: AGROBACTERIUM TUMEFACIENS
• Cellular location: Cell inner membrane; Single-pass membrane protein (Potential): P17798
• Total number of polymer chains: 2
• Total formula weight: 33943.83

Authors

Bailey, S.,Ward, D.,Middleton, R.,Grossmann, G.,Zambryski, P.C. (deposition date: 2006-01-11, release date: 2006-01-30, Last modification date: 2023-12-13)

Primary citation

Bailey, S.,Ward, D.,Middleton, R.,Grossmann, J.G.,Zambryski, P.C.
Agrobacterium Tumefaciens Virb8 Structure Reveals Potential Protein-Protein Interactions Sites.
Proc.Natl.Acad.Sci.USA, 103:2582-, 2006

PubMed Abstract: 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.

PubMed: 16481621
DOI: 10.1073/PNAS.0511216103

Experimental method

X-RAY DIFFRACTION (2.2 Å)