3prp

Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin

spinqualitylabelsall models 3prp, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3prp is a 4 chain structure with sequence from Homo sapiens and Orthonairovirus haemorrhagiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.699Å Ligands: 4LJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L_CCHFI Displays RNA-directed RNA polymerase, deubiquitinating and deISGylase activities. RNA-dependent RNA polymerase is responsible for replication and transcription of the viral RNA genome. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent innate immunity. Publication Abstract from PubMed Crimean-Congo hemorrhagic fever (CCHF) virus is a tick borne ssRNA (-) nairovirus that produces fever, prostration, and severe hemorrhages in humans. With fatality rates for CCHF ranging up to 70% based on several factors, CCHF is considered a dangerous emerging disease. Originally identified in the former U.S.S.R. and the Congo, CCHF has rapidly spread across large sections of Europe, Asia, and Africa. Recent reports have identified a viral homologue of the ovarian tumor protease superfamily (vOTU) within its L-protein. This protease has subsequently been implicated in down-regulation of the interferon type 1 immune response through cleavage of post-translational modifying proteins ubiquitin (Ub) and Ub-like interferon-simulated gene 15 (ISG15). Additionally, homologues of vOTU have been suggested to perform similar roles in the ssRNA (+) Arteriviruses. By utilizing X-ray crystallographic techniques, the structure of vOTU covalently bound to ubiquitin propylamine, a suicide substrate of the enzyme, was elucidated to 1.7 A revealing unique structural elements that define this new subclass of the OTU superfamily. In additions, kinetic studies were carried out with aminomethylcoumarin (AMC) conjugates of monomeric Ub, ISG15, and Neural precursor cell expressed, developmentally down-regulated 8 (NEDD8) substrates in order to provide quantitative insight into vOTU's preference of Ub and Ub-like substrates. Structural analysis of a viral ovarian tumor domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with covalently bonded ubiquitin.,Capodagli GC, McKercher MA, Baker EA, Masters EM, Brunzelle JS Dr, Pegan SD Dr J Virol. 2011 Jan 12. PMID:21228232 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of ubiquitin

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