2cc3

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==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Middleton, R.]]
[[Category: Middleton, R.]]
[[Category: Ward, D.]]
[[Category: Ward, D.]]
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[[Category: Zambryski, P.C.]]
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[[Category: Zambryski, P C.]]
[[Category: MPD]]
[[Category: MPD]]
[[Category: agrobacterium]]
[[Category: agrobacterium]]
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[[Category: virb8]]
[[Category: virb8]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:33:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:08 2008''

Revision as of 14:47, 21 February 2008


2cc3, resolution 2.20Å

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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 as ligand. Known structural/functional Site: . 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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