2oiv
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(New page: 200px<br /><applet load="2oiv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oiv, resolution 1.95Å" /> '''Structural Analysis ...)
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Revision as of 13:07, 23 January 2008
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Structural Analysis of Xanthomonas XopD Provides Insights Into Substrate Specificity of Ubiquitin-like Protein Proteases
Overview
XopD (Xanthomonas outer protein D), a type III secreted effector from, Xanthomonas campestris pv. vesicatoria, is a desumoylating enzyme with, strict specificity for its plant small ubiquitin-like modifier (SUMO), substrates. Based on SUMO sequence alignments and peptidase assays with, various plant, yeast, and mammalian SUMOs, we identified residues in SUMO, that contribute to XopD/SUMO recognition. Further predictions regarding, the enzyme/substrate specificity were made by solving the XopD crystal, structure. By incorporating structural information with sequence, alignments and enzyme assays, we were able to elucidate determinants of, the rigid SUMO specificity exhibited by the Xanthomonas virulence factor, XopD.
About this Structure
2OIV is a Single protein structure of sequence from Xanthomonas euvesicatoria with as ligand. Full crystallographic information is available from OCA.
Reference
Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases., Chosed R, Tomchick DR, Brautigam CA, Mukherjee S, Negi VS, Machius M, Orth K, J Biol Chem. 2007 Mar 2;282(9):6773-82. Epub 2007 Jan 3. PMID:17204475
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