2izp
From Proteopedia
(New page: 200px<br /><applet load="2izp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2izp, resolution 2.1Å" /> '''BIPD- AN INVASION PRT...) |
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==Overview== | ==Overview== | ||
| - | Burkoldheria pseudomallei is a Gram-negative bacterium that possesses a | + | Burkoldheria pseudomallei is a Gram-negative bacterium that possesses a protein secretion system similar to those found in Salmonella and Shigella. Recent work has indicated that the protein encoded by the BipD gene of B. pseudomallei is an important secreted virulence factor. BipD is similar in sequence to IpaD from Shigella and SipD from Salmonella and is therefore likely to be a translocator protein in the type-III secretion system of B. pseudomallei. The crystal structure of BipD has been solved at a resolution of 2.1 A revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel alpha-helical segments with two small beta-sheet regions. The longest helices of the molecule form a four-helix bundle and most of the remaining secondary structure elements (three helices and two three-stranded beta-sheets) are formed by the region linking the last two helices of the four-helix bundle. The structure suggests that the biologically active form of the molecule may be a dimer formed by contacts involving the C-terminal alpha-helix, which is the most strongly conserved part of the protein. Comparison of the structure of BipD with immunological and other data for IpaD indicates that the C-terminal alpha-helix is also involved in contacts with other proteins that form the translocon. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
| - | [[Category: Erskine, P | + | [[Category: Erskine, P T.]] |
| - | [[Category: Fox, G | + | [[Category: Fox, G C.]] |
[[Category: Gill, R.]] | [[Category: Gill, R.]] | ||
| - | [[Category: Knight, M | + | [[Category: Knight, M J.]] |
[[Category: Mikolajek, H.]] | [[Category: Mikolajek, H.]] | ||
[[Category: Ruaux, A.]] | [[Category: Ruaux, A.]] | ||
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[[Category: Wong-Fat-Sang, N.]] | [[Category: Wong-Fat-Sang, N.]] | ||
[[Category: Wood, M.]] | [[Category: Wood, M.]] | ||
| - | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
[[Category: invasion protein]] | [[Category: invasion protein]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
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[[Category: virulence factor]] | [[Category: virulence factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:42 2008'' |
Revision as of 15:57, 21 February 2008
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BIPD- AN INVASION PRTEIN ASSOCIATED WITH THE TYPE-III SECRETION SYSTEM OF BURKHOLDERIA PSEUDOMALLEI.
Overview
Burkoldheria pseudomallei is a Gram-negative bacterium that possesses a protein secretion system similar to those found in Salmonella and Shigella. Recent work has indicated that the protein encoded by the BipD gene of B. pseudomallei is an important secreted virulence factor. BipD is similar in sequence to IpaD from Shigella and SipD from Salmonella and is therefore likely to be a translocator protein in the type-III secretion system of B. pseudomallei. The crystal structure of BipD has been solved at a resolution of 2.1 A revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel alpha-helical segments with two small beta-sheet regions. The longest helices of the molecule form a four-helix bundle and most of the remaining secondary structure elements (three helices and two three-stranded beta-sheets) are formed by the region linking the last two helices of the four-helix bundle. The structure suggests that the biologically active form of the molecule may be a dimer formed by contacts involving the C-terminal alpha-helix, which is the most strongly conserved part of the protein. Comparison of the structure of BipD with immunological and other data for IpaD indicates that the C-terminal alpha-helix is also involved in contacts with other proteins that form the translocon.
About this Structure
2IZP is a Single protein structure of sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA.
Reference
High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei., Erskine PT, Knight MJ, Ruaux A, Mikolajek H, Wong Fat Sang N, Withers J, Gill R, Wood SP, Wood M, Fox GC, Cooper JB, J Mol Biol. 2006 Oct 13;363(1):125-36. Epub 2006 Aug 1. PMID:16950399
Page seeded by OCA on Thu Feb 21 17:57:42 2008
