3u9b | pdb_00003u9b

Structure of apo-CATI

spinqualitylabelsall models 3u9b, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u9b is a 9 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3u9f Gene: cat ("Bacillus coli" Migula 1895) Activity: Chloramphenicol O-acetyltransferase, with EC number 2.3.1.28 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAT_ECOLX] This enzyme is an effector of chloramphenicol resistance in bacteria. Publication Abstract from PubMed Novel antibiotics are needed to overcome the challenge of continually evolving bacterial resistance. This has led to a renewed interest in mechanistic studies of once popular antibiotics like chloramphenicol (CAM). Chloramphenicol acetyltransferases (CATs) are enzymes that covalently modify CAM, rendering it inactive against its target, the ribosome, and thereby causing resistance to CAM. Out of the three major types of CAT (CAT(I-III) ), the CAM-specific CAT(III) has been studied extensively. Much less is known about another clinically important type, CAT(I) . In addition to inactivating CAM and unlike CAT(III) , CAT(I) confers resistance to a structurally distinct antibiotic, fusidic acid (FA). The origin of the broader substrate specificity of CAT(I) has not been fully elucidated. To understand the substrate binding features of CAT(I) , its crystal structures in the unbound (apo) and CAM-bound forms were determined. The analysis of these and previously determined CAT(I) -FA and CAT(III) -CAM structures revealed interactions responsible for CAT(I) binding to its substrates and clarified the broader substrate preference of CAT(I) compared to that of CAT(III) . The structural basis for substrate versatility of chloramphenicol acetyltransferase CAT(I).,Biswas T, Houghton JL, Garneau-Tsodikova S, Tsodikov OV Protein Sci. 2012 Jan 31. doi: 10.1002/pro.2036. PMID:22294317 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chloramphenicol acetyltransferase 3D structures

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