6r0r

Getah virus macro domain in complex with ADPr covalently bond to Cys34

spinqualitylabelsall models 6r0r, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r0r is a 1 chain structure with sequence from Getah virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: EDO, JNT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Alphaviruses are (re-)emerging arboviruses of public health concern. The nsP3 gene product is one of the key players during viral replication. NsP3 comprises three domains: a macro domain, a zinc-binding domain and a hypervariable region. The macro domain is essential at both early and late stages of the replication cycle through ADP-ribose (ADPr) binding and de-ADP-ribosylation of host proteins. However, both its specific role and the precise molecular mechanism of de-ADP-ribosylation across specific viral families remains to be elucidated. Here we investigate by X-ray crystallography the mechanism of ADPr reactivity in the active site of Getah virus macro domain, which displays a peculiar substitution of one of the conserved residues in the catalytic loop. ADPr adopts distinct poses including a covalent bond between the C1 of the ADPr and a conserved Togaviridae-specific cysteine. These different poses observed for ADPr may represent snapshots of the de-ADP-ribosylation mechanism, highlighting residues to be further characterised. Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.,Ferreira-Ramos AS, Sulzenbacher G, Canard B, Coutard B Sci Rep. 2020 Sep 2;10(1):14422. doi: 10.1038/s41598-020-70870-w. PMID:32879358 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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