9g7g

Structure of the clippase PaJOS from Pigmentiphaga aceris

spinqualitylabelsall models 9g7g, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9g7g is a 24 chain structure with sequence from Homo sapiens and Pigmentiphaga aceris. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.89Å Ligands: AYE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A5C0B1L0_9BURK Publication Abstract from PubMed Many intracellular bacteria secrete deubiquitinase (DUB) effectors into eukaryotic host cells to keep the bacterial surface or the enclosing vesicle membrane free of ubiquitin marks. This study describes a family of DUBs from several bacterial genera, including Simkania, Parachlamydia, Burkholderia, and Pigmentiphaga, which is structurally related to eukaryotic Josephin-type DUBs but contains members that catalyze a unique destructive substrate deubiquitination. These ubiquitin C-terminal clippases (UCCs) cleave ubiquitin before the C-terminal diGly motif, thereby truncating the modifier and leaving a remnant on the substrate. By comparing the crystal structures of substrate-bound clippases and a closely related conventional DUB, we identified the factors causing this shift and found them to be conserved in other clippases, including one highly specific for M1-linked ubiquitin chains. This enzyme class has great potential to serve as tools for studying the ubiquitin system, particularly aspects involving branched chains. A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode.,Hermanns T, Kolek S, Uthoff M, de Heiden RA, Mulder MPC, Baumann U, Hofmann K Mol Cell. 2025 Mar 20;85(6):1202-1215.e5. doi: 10.1016/j.molcel.2025.02.002. Epub , 2025 Mar 3. PMID:40037356 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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