5x5m
From Proteopedia
Crystal structure of a hydrolase encoded by lin2189 from Listeria innocua
Structural highlights
FunctionPublication Abstract from PubMedGyrI-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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