Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases.
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.
Chosed
Renee
R
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9148, USA.
Tomchick
Diana R
DR
Brautigam
Chad A
CA
Mukherjee
Sohini
S
Negi
Veera S
VS
Machius
Mischa
M
Orth
Kim
K
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D016415:Sequence Alignment; D025841:Small Ubiquitin-Related Modifier Proteins / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity; D037521:Virulence Factors / Q000737:chemistry; D014974:Xanthomonas / Q000737:chemistry*
D001425:Bacterial Outer Membrane Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; D037521:Virulence Factors