5x5m | pdb_00005x5m

Crystal structure of a hydrolase encoded by lin2189 from Listeria innocua

spinqualitylabelsall models 5x5m, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x5m is a 2 chain structure with sequence from Listeria innocua Clip11262. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.211Å Ligands: 7YU, DMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q929T5_LISIN Publication Abstract from PubMed GyrI-like proteins are widely distributed in prokaryotes and eukaryotes, and recognized as small-molecule binding proteins. Here, we identify a subfamily of these proteins as cyclopropanoid cyclopropyl hydrolases (CCHs) that can catalyze the hydrolysis of the potent DNA-alkylating agents yatakemycin (YTM) and CC-1065. Co-crystallography and molecular dynamics simulation analyses reveal that these CCHs share a conserved aromatic cage for the hydrolytic activity. Subsequent cytotoxic assays confirm that CCHs are able to protect cells against YTM. Therefore, our findings suggest that the evolutionarily conserved GyrI-like proteins confer cellular protection against diverse xenobiotics via not only binding, but also catalysis. GyrI-like proteins catalyze cyclopropanoid hydrolysis to confer cellular protection.,Yuan H, Zhang J, Cai Y, Wu S, Yang K, Chan HCS, Huang W, Jin WB, Li Y, Yin Y, Igarashi Y, Yuan S, Zhou J, Tang GL Nat Commun. 2017 Nov 14;8(1):1485. doi: 10.1038/s41467-017-01508-1. PMID:29133784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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