2OIV
Structural Analysis of Xanthomonas XopD Provides Insights Into Substrate Specificity of Ubiquitin-like Protein Proteases
Summary for 2OIV
| Entry DOI | 10.2210/pdb2oiv/pdb |
| Related | 2OIX |
| Descriptor | Xanthomonas outer protein D, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | clan ce family 48 cysteine protease, type iii secreted effector, desumoylating enzyme, secreted virulence factor, peptidase, isopeptidase, hydrolase |
| Biological source | Xanthomonas euvesicatoria |
| Total number of polymer chains | 1 |
| Total formula weight | 20858.09 |
| Authors | Chosed, R.,Tomchick, D.R.,Brautigam, C.A.,Machius, M.,Orth, K. (deposition date: 2007-01-11, release date: 2007-05-29, Last modification date: 2023-12-27) |
| Primary citation | Chosed, R.,Tomchick, D.R.,Brautigam, C.A.,Mukherjee, S.,Negi, V.S.,Machius, M.,Orth, K. Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases. J.Biol.Chem., 282:6773-6782, 2007 Cited by PubMed Abstract: 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. PubMed: 17204475DOI: 10.1074/jbc.M608730200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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