The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase

Abstract

The Mycobacterium tuberculosis enzyme Rv2275 catalyzes the formation of cyclo(L-Tyr-L-Tyr) using two molecules of Tyr-tRNA(Tyr) as substrates. The three-dimensional (3D) structure of Rv2275 was determined to 2.0-Å resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl-tRNA synthetase family of enzymes. Mutagenesis and radioactive labeling suggests a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNA(Tyr) to an active site serine (Ser88) by transesterification with Glu233 serving as a critical base, catalyzing dipeptide bond formation.

DOI: 10.1038/nchembio.440

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@inproceedings{Vetting2010TheSA, title={The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase}, author={Matthew W. Vetting and Subray S. Hegde and John S Blanchard}, booktitle={Nature chemical biology}, year={2010} }