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Title: Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei

Abstract

BipD is likely to be a component of a type-III protein secretion system (TTSS) in B. pseudomallei. Native and selenomethionyl-BipD proteins have been expressed and crystals have been obtained which diffract to 2.1 Å. Burkholderia pseudomallei, the causative agent of melioidosis, possesses a protein-secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to secrete virulence-associated proteins into target cells of the host organism. The BipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and most likely functionally analogous to IpaD from Shigella and SipD from Salmonella. Thus, the BipD protein is likely to be a component of a type III protein-secretion system (TTSS) in B. pseudomallei. Proteins in the same class as BipD, such as IpaD and SipD, are thought to act as extracellular chaperones to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and might even link the translocon pore with the secretion needle. There is evidence that the translocator proteins also bind an integrin which stimulates actin-mediated insertion of the bacterium into the host-cell membrane. Native BipD has been crystallized in a monoclinic crystalmore » form that diffracts X-rays to 2.5 Å resolution. BipD protein which incorporates selenomethionine (SeMet-BipD) has also been expressed and forms crystals which diffract to a higher resolution of 2.1 Å.« less

Authors:
; ; ; ; ;  [1];  [2]
  1. School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX (United Kingdom)
  2. Institute of Animal Health, Division of Environmental Microbiology, Institute for Animal Health, Compton Laboratory, Berkshire RG20 7NN (United Kingdom)
Publication Date:
OSTI Identifier:
22360177
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 62; Journal Issue: Pt 8; Other Information: PMCID: PMC2242920; PMID: 16880550; PUBLISHER-ID: fw5094; OAI: oai:pubmedcentral.nih.gov:2242920; Copyright (c) International Union of Crystallography 2006; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; EQUIPMENT; RESOLUTION; X-RAY DIFFRACTION

Citation Formats

Knight, M. J., Ruaux, A., Mikolajek, H., Erskine, P. T., Gill, R., Wood, S. P., Wood, M., and Cooper, J. B., E-mail: j.b.cooper@soton.ac.uk. Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106024857.
Knight, M. J., Ruaux, A., Mikolajek, H., Erskine, P. T., Gill, R., Wood, S. P., Wood, M., & Cooper, J. B., E-mail: j.b.cooper@soton.ac.uk. Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei. United Kingdom. doi:10.1107/S1744309106024857.
Knight, M. J., Ruaux, A., Mikolajek, H., Erskine, P. T., Gill, R., Wood, S. P., Wood, M., and Cooper, J. B., E-mail: j.b.cooper@soton.ac.uk. Tue . "Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei". United Kingdom. doi:10.1107/S1744309106024857.
@article{osti_22360177,
title = {Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor from Burkholderia pseudomallei},
author = {Knight, M. J. and Ruaux, A. and Mikolajek, H. and Erskine, P. T. and Gill, R. and Wood, S. P. and Wood, M. and Cooper, J. B., E-mail: j.b.cooper@soton.ac.uk},
abstractNote = {BipD is likely to be a component of a type-III protein secretion system (TTSS) in B. pseudomallei. Native and selenomethionyl-BipD proteins have been expressed and crystals have been obtained which diffract to 2.1 Å. Burkholderia pseudomallei, the causative agent of melioidosis, possesses a protein-secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to secrete virulence-associated proteins into target cells of the host organism. The BipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and most likely functionally analogous to IpaD from Shigella and SipD from Salmonella. Thus, the BipD protein is likely to be a component of a type III protein-secretion system (TTSS) in B. pseudomallei. Proteins in the same class as BipD, such as IpaD and SipD, are thought to act as extracellular chaperones to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and might even link the translocon pore with the secretion needle. There is evidence that the translocator proteins also bind an integrin which stimulates actin-mediated insertion of the bacterium into the host-cell membrane. Native BipD has been crystallized in a monoclinic crystal form that diffracts X-rays to 2.5 Å resolution. BipD protein which incorporates selenomethionine (SeMet-BipD) has also been expressed and forms crystals which diffract to a higher resolution of 2.1 Å.},
doi = {10.1107/S1744309106024857},
journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 8,
volume = 62,
place = {United Kingdom},
year = {2006},
month = {8}
}