Crystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6

Ve, Thomas, Williams, Simon, Valkov, Eugene, Ellis, Jeffrey G., Dodds, Peter N. and Kobe, Bostjan (2011) Crystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, 67 2: 237-240. doi:10.1107/S1744309110051006

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Author Ve, Thomas
Williams, Simon
Valkov, Eugene
Ellis, Jeffrey G.
Dodds, Peter N.
Kobe, Bostjan
Title Crystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6
Journal name Acta Crystallographica. Section F: Structural Biology and Crystallization Communications   Check publisher's open access policy
ISSN 1744-3091
Publication date 2011-02
Sub-type Article (original research)
DOI 10.1107/S1744309110051006
Open Access Status File (Publisher version)
Volume 67
Issue 2
Start page 237
End page 240
Total pages 4
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Collection year 2012
Language eng
Formatted abstract
The Toll/interleukin-1 receptor (TIR) domain is a protein–protein interaction domain that is found in both animal and plant immune receptors. In animal Tolllike receptor signalling, both homotypic TIR-domain interactions between two receptor molecules and heterotypic interactions between receptors and TIRdomain-containing adaptors are required for initiation of an innate immune response. The TIR domains in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant disease-resistance proteins are not as well characterized, but recent studies have suggested a role in defence signalling. In this study, the crystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6 (L6TIR) are reported. Plate-like crystals of L6TIR were obtained using PEG 200 as a precipitant and diffracted X-rays to 2.3 Â resolution. Pseudo-translation complicated the initial assignment of the crystal symmetry, which was ultimately found to correspond to space group P21212 with two molecules per asymmetric unit. The structure of L6TIR was solved by molecular replacement using the structure of the TIR-domain-containing protein AT1G72930 from Arabidopsis as a template.
Keyword For-gene specificity
Crystal-structure
Avirulence genes
Arabidopsis
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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Created: Sun, 20 Mar 2011, 00:14:26 EST