2X9Q
Structure of the Mycobacterium tuberculosis protein, Rv2275, demonstrates that cyclodipeptide synthetases are related to type I tRNA-Synthetases.
Summary for 2X9Q
| Entry DOI | 10.2210/pdb2x9q/pdb |
| Descriptor | CYCLODIPEPTIDE SYNTHETASE (2 entities in total) |
| Functional Keywords | ligase |
| Biological source | MYCOBACTERIUM TUBERCULOSIS |
| Total number of polymer chains | 2 |
| Total formula weight | 63803.80 |
| Authors | Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. (deposition date: 2010-03-23, release date: 2010-09-22, Last modification date: 2024-11-06) |
| Primary citation | Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. The Structure and Mechanism of the Mycobacterium Tuberculosis Cyclodityrosine Synthetase. Nat.Chem.Biol., 6:797-, 2010 Cited by PubMed 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. PubMed: 20852636DOI: 10.1038/NCHEMBIO.440 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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