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Structure of chloramphenicol acetyltransferase at 1.75-A resolution.

Chloramphenicol acetyltransferase [acetyl-CoA:chloramphenicol O3-acetyltransferase; EC 2.3.1.28] is the enzyme responsible for high-level bacterial resistance to the antibiotic chloramphenicol. It catalyzes the transfer of an acetyl group from acetyl CoA to the primary hydroxyl of chloramphenicol. The x-ray crystallographic structure of the type III variant enzyme from Escherichia coli has been determined and refined at 1.75-A resolution. The enzyme is a trimer of identical subunits with a distinctive protein fold. Structure of the trimer is stabilized by a beta-pleated sheet that extends from one subunit to the next. The active site is located at the subunit interface, and the binding sites for both chloramphenicol and CoA have been characterized. Substrate binding is unusual in that the two substrates approach the active site via clefts on opposite molecular "sides." A histidine residue previously implicated in catalysis is appropriately positioned to act as a general base catalyst in the reaction.[1]

References

  1. Structure of chloramphenicol acetyltransferase at 1.75-A resolution. Leslie, A.G., Moody, P.C., Shaw, W.V. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
 
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