Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases

Renee Chosed, Diana R Tomchick, Chad A Brautigam, Sohini Mukherjee, Veera S. Negi, Mischa Machius, Kim A Orth

Research output: Contribution to journalArticle

55 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)6773-6782
Number of pages10
JournalJournal of Biological Chemistry
Volume282
Issue number9
DOIs
StatePublished - Mar 2 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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