2cc3: Difference between revisions

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.

2CC3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CC3 OCA].  

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