2bhv: Difference between revisions

Revision as of 17:38, 21 February 2008

STRUCTURE OF COMB10 OF THE COM TYPE IV SECRETION SYSTEM OF HELICOBACTER PYLORI

OverviewOverview

Type IV secretion systems (T4SSs) are commonly used secretion machineries in Gram-negative bacteria. They are used in the infection of human, animal, or plant cells and the propagation of antibiotic resistance. The T4SS apparatus spans both membranes of the bacterium and generally is composed of 12 proteins, named VirB1-11 and VirD4 after proteins of the canonical Agrobacterium tumefaciens T4SS. The periplasmic core complex of VirB8/VirB10 structurally and functionally links the cytoplasmic NTPases of the system with its outer membrane and pilus components. Here we present crystal structures of VirB8 of Brucella suis, the causative agent of brucellosis, and ComB10, a VirB10 homolog of Helicobacter pylori, the causative agent of gastric ulcers. The structures of VirB8 and ComB10 resemble known folds, albeit with novel secondary-structure modifications unique to and conserved within their respective families. Both proteins crystallized as dimers, providing detailed predictions about their self associations. These structures make a substantial contribution to the repertoire of T4SS component structures and will serve as springboards for future functional and protein-protein interaction studies by using knowledge-based site-directed and deletion mutagenesis.

About this StructureAbout this Structure

2BHV is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

ReferenceReference

Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori., Terradot L, Bayliss R, Oomen C, Leonard GA, Baron C, Waksman G, Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4596-601. Epub 2005 Mar 11. PMID:15764702

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 ==Overview==
-Type IV secretion systems (T4SSs) are commonly used secretion machineries, in Gram-negative bacteria. They are used in the infection of human, animal, or plant cells and the propagation of antibiotic resistance. The, T4SS apparatus spans both membranes of the bacterium and generally is, composed of 12 proteins, named VirB1-11 and VirD4 after proteins of the, canonical Agrobacterium tumefaciens T4SS. The periplasmic core complex of, VirB8/VirB10 structurally and functionally links the cytoplasmic NTPases, of the system with its outer membrane and pilus components. Here we, present crystal structures of VirB8 of Brucella suis, the causative agent, of brucellosis, and ComB10, a VirB10 homolog of Helicobacter pylori, the, causative agent of gastric ulcers. The structures of VirB8 and ComB10, resemble known folds, albeit with novel secondary-structure modifications, unique to and conserved within their respective families. Both proteins, crystallized as dimers, providing detailed predictions about their self, associations. These structures make a substantial contribution to the, repertoire of T4SS component structures and will serve as springboards for, future functional and protein-protein interaction studies by using, knowledge-based site-directed and deletion mutagenesis.
+Type IV secretion systems (T4SSs) are commonly used secretion machineries in Gram-negative bacteria. They are used in the infection of human, animal, or plant cells and the propagation of antibiotic resistance. The T4SS apparatus spans both membranes of the bacterium and generally is composed of 12 proteins, named VirB1-11 and VirD4 after proteins of the canonical Agrobacterium tumefaciens T4SS. The periplasmic core complex of VirB8/VirB10 structurally and functionally links the cytoplasmic NTPases of the system with its outer membrane and pilus components. Here we present crystal structures of VirB8 of Brucella suis, the causative agent of brucellosis, and ComB10, a VirB10 homolog of Helicobacter pylori, the causative agent of gastric ulcers. The structures of VirB8 and ComB10 resemble known folds, albeit with novel secondary-structure modifications unique to and conserved within their respective families. Both proteins crystallized as dimers, providing detailed predictions about their self associations. These structures make a substantial contribution to the repertoire of T4SS component structures and will serve as springboards for future functional and protein-protein interaction studies by using knowledge-based site-directed and deletion mutagenesis.
 ==About this Structure==
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 [[Category: bacterial type iv secretion]]
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