The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase

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 structure of Rv2275 was determined to 2.0 Å resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl-tRNA-sy...

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Autores principales: Vetting, Matthew W., Hegde, Subray S., Blanchard, John S.
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2957485/
https://www.ncbi.nlm.nih.gov/pubmed/20852636
http://dx.doi.org/10.1038/nchembio.440
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author Vetting, Matthew W.
Hegde, Subray S.
Blanchard, John S.
author_facet Vetting, Matthew W.
Hegde, Subray S.
Blanchard, John S.
author_sort Vetting, Matthew W.
collection PubMed
description 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 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 (S88) by transesterification and with E233 serving as a critical base catalyzing dipeptide bond formation.
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spelling pubmed-29574852011-05-01 The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase Vetting, Matthew W. Hegde, Subray S. Blanchard, John S. Nat Chem Biol Article 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 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 (S88) by transesterification and with E233 serving as a critical base catalyzing dipeptide bond formation. 2010-09-19 2010-11 /pmc/articles/PMC2957485/ /pubmed/20852636 http://dx.doi.org/10.1038/nchembio.440 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Vetting, Matthew W.
Hegde, Subray S.
Blanchard, John S.
The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title_full The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title_fullStr The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title_full_unstemmed The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title_short The Structure and Mechanism of the Mycobacterium tuberculosis Cyclodityrosine Synthetase
title_sort structure and mechanism of the mycobacterium tuberculosis cyclodityrosine synthetase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2957485/
https://www.ncbi.nlm.nih.gov/pubmed/20852636
http://dx.doi.org/10.1038/nchembio.440
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