5jp1 | pdb_00005jp1

Structure of Xanthomonas campestris effector protein XopD bound to tomato SUMO

spinqualitylabelsall models 5jp1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jp1 is a 2 chain structure with sequence from Solanum lycopersicum and Xanthomonas campestris pv. vesicatoria str. 85-10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: AYE, D1D, MLI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3BYJ5_XANC5 Publication Abstract from PubMed Pathogenic bacteria rely on secreted effector proteins to manipulate host signaling pathways, often in creative ways. CE clan proteases, specific hydrolases for ubiquitin-like modifications (SUMO and NEDD8) in eukaryotes, reportedly serve as bacterial effector proteins with deSUMOylase, deubiquitinase, or, even, acetyltransferase activities. Here, we characterize bacterial CE protease activities, revealing K63-linkage-specific deubiquitinases in human pathogens, such as Salmonella, Escherichia, and Shigella, as well as ubiquitin/ubiquitin-like cross-reactive enzymes in Chlamydia, Rickettsia, and Xanthomonas. Five crystal structures, including ubiquitin/ubiquitin-like complexes, explain substrate specificities and redefine relationships across the CE clan. Importantly, this work identifies novel family members and provides key discoveries among previously reported effectors, such as the unexpected deubiquitinase activity in Xanthomonas XopD, contributed by an unstructured ubiquitin binding region. Furthermore, accessory domains regulate properties such as subcellular localization, as exemplified by a ubiquitin-binding domain in Salmonella Typhimurium SseL. Our work both highlights and explains the functional adaptations observed among diverse CE clan proteins. The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.,Pruneda JN, Durkin CH, Geurink PP, Ovaa H, Santhanam B, Holden DW, Komander D Mol Cell. 2016 Jul 21;63(2):261-76. doi: 10.1016/j.molcel.2016.06.015. Epub 2016 , Jul 14. PMID:27425412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also SUMO 3D Structures

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