2x9q | pdb_00002x9q
Structure of the Mycobacterium tuberculosis protein, Rv2275, demonstrates that cyclodipeptide synthetases are related to type I tRNA-Synthetases.
Structural highlights
Function[CDTS_MYCTU] Involved in the biosynthesis of mycocyclosin. It uses activated amino acids in the form of aminoacyl-tRNAs (aa-tRNAs) as substrates to catalyze the ATP-independent formation of cyclodipeptides which are intermediates in diketopiperazine (DKP) biosynthetic pathways. Catalyzes the formation of cyclo(L-Tyr-L-Tyr) (cYY) from L-tyrosyl-tRNA(Tyr). Can incorporate various nonpolar residues, such as L-phenylalanine, L-leucine, L-tyrosine and L-methionine, and to a much lesser extent L-alanine, into cyclodipeptides. Cyclodipeptides synthesized by Rv2275 always contain L-tyrosine.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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-A 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. The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase.,Vetting MW, Hegde SS, Blanchard JS Nat Chem Biol. 2010 Sep 19. PMID:20852636[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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