Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB

Alaidarous, Mohammed, Ve, Thomas, Ullah, M. Obayed, Valkov, Eugene, Mansell, Ashley, Schembri, Mark A., Sweet, Matthew J. and Kobe, Bostjan (2013) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69 10: 1167-1170. doi:10.1107/S1744309113024408

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Author Alaidarous, Mohammed
Ve, Thomas
Ullah, M. Obayed
Valkov, Eugene
Mansell, Ashley
Schembri, Mark A.
Sweet, Matthew J.
Kobe, Bostjan
Title Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB
Formatted title
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB
Journal name Acta Crystallographica Section F: Structural Biology and Crystallization Communications   Check publisher's open access policy
ISSN 1744-3091
Publication date 2013-10
Year available 2013
Sub-type Article (original research)
DOI 10.1107/S1744309113024408
Open Access Status File (Author Post-print)
Volume 69
Issue 10
Start page 1167
End page 1170
Total pages 4
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell Publishing
Collection year 2014
Language eng
Formatted abstract
In mammals, Toll-like receptors (TLRs) recognize conserved microbial molecular signatures and induce an early innate immune response in the host. TLR signalling is mediated by interactions between the cytosolic TIR (Toll/interleukin-1 receptor) domains of the receptor and the adaptor proteins. Increasingly, it is apparent that pathogens target this interaction via pathogen-expressed TIR-domain-containing proteins to modulate immune responses. A TIR-domain-containing protein TcpB has been reported in the pathogenic bacterium Brucella melitensis. Studies have shown that TcpB interferes with the TLR2 and TLR4 signalling pathways to inhibit TLR-mediated inflammatory responses. Such interference may involve TIR-TIR-domain interactions between bacterial and mammalian proteins, but there is a lack of information about these interactions at the molecular level. In this study, the cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the protein construct corresponding to the TIR domain of TcpB (residues 120-250) are reported. The crystals diffracted to 2.6 Å resolution, have the symmetry of the monoclinic space group P21 and are most likely to contain four molecules in the asymmetric unit. The structure should help in understanding the molecular basis of how TcpB affects the innate immunity of the host.
Keyword Toll-like receptors
Innate immunity
TIR domain
Brucella spp.
TcpB
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Fri, 11 Oct 2013, 10:40:05 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences