The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase

Matthew W. Vetting, Subray Hegde, John S. Blanchard

Research output: Contribution to journalArticle

46 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)797-799
Number of pages3
JournalNature Chemical Biology
Volume6
Issue number11
DOIs
StatePublished - Nov 2010

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RNA, Transfer, Tyr
Ligases
Mycobacterium tuberculosis
Amino Acyl-tRNA Synthetases
Dipeptides
Enzymes
Mutagenesis
Serine
Tyrosine
Catalytic Domain

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. / Vetting, Matthew W.; Hegde, Subray; Blanchard, John S.

In: Nature Chemical Biology, Vol. 6, No. 11, 11.2010, p. 797-799.

Research output: Contribution to journalArticle

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