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High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei

High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei
High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei
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 Å revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel α-helical segments with two small β-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 β-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 α-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 α-helix is also involved in contacts with other proteins that form the translocon.
type-III secretion system, invasion protein, BipD, burkholderia pseudomallei, x-ray structure
0022-2836
125-136
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Knight, M.J.
3f836d6c-f83f-41bd-a2f4-4da770ac1e8d
Ruaux, A.
e079ff49-40e7-4866-8f4c-8087e1224db5
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Wong Fat Sang, N.
cde43428-0bca-48c7-b0c4-4cdb59dc8310
Withers, J.
eb84a07f-a53b-4633-8056-63abe1282549
Gill, R.
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Wood, S.P.
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Wood, M.
e80db4b2-cf82-4044-a37c-2e23c031e14e
Fox, G.C.
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Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Knight, M.J.
3f836d6c-f83f-41bd-a2f4-4da770ac1e8d
Ruaux, A.
e079ff49-40e7-4866-8f4c-8087e1224db5
Mikolajek, H.
c394c255-9248-4217-ace9-4a0382bfc0c5
Wong Fat Sang, N.
cde43428-0bca-48c7-b0c4-4cdb59dc8310
Withers, J.
eb84a07f-a53b-4633-8056-63abe1282549
Gill, R.
95656ecb-604f-425e-ac66-7dd36e47d94d
Wood, S.P.
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Wood, M.
e80db4b2-cf82-4044-a37c-2e23c031e14e
Fox, G.C.
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Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0

Erskine, P.T., Knight, M.J., Ruaux, A., Mikolajek, H., Wong Fat Sang, N., Withers, J., Gill, R., Wood, S.P., Wood, M., Fox, G.C. and Cooper, J.B. (2006) High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei. Journal of Molecular Biology, 363 (1), 125-136. (doi:10.1016/j.jmb.2006.07.069). (PMID:16950399)

Record type: Article

Abstract

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 Å revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel α-helical segments with two small β-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 β-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 α-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 α-helix is also involved in contacts with other proteins that form the translocon.

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Submitted date: 29 May 2006
e-pub ahead of print date: 1 August 2006
Published date: 13 October 2006
Keywords: type-III secretion system, invasion protein, BipD, burkholderia pseudomallei, x-ray structure

Identifiers

Local EPrints ID: 43196
URI: http://eprints.soton.ac.uk/id/eprint/43196
ISSN: 0022-2836
PURE UUID: e84acde1-da38-4857-9759-80762ce4785c
ORCID for H. Mikolajek: ORCID iD orcid.org/0000-0003-0776-9974

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Date deposited: 15 Jan 2007
Last modified: 15 Mar 2024 08:53

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Contributors

Author: P.T. Erskine
Author: M.J. Knight
Author: A. Ruaux
Author: H. Mikolajek ORCID iD
Author: N. Wong Fat Sang
Author: J. Withers
Author: R. Gill
Author: S.P. Wood
Author: M. Wood
Author: G.C. Fox
Author: J.B. Cooper

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