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Literature summary extracted from

  • Sankaranarayanan, R.; Cherney, M.M.; Garen, C.; Garen, G.; Niu, C.; Yuan, M.; James, M.N.
    The molecular structure of ornithine acetyltransferase from Mycobacterium tuberculosis bound to ornithine, a competitive inhibitor (2010), J. Mol. Biol., 397, 979-990.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.35 crystal structures of Mtb OAT in native form and in its complex with ornithine has been determined at 1.7 and 2.4 A resolutions, respectively. Ornithine binding does not alter the structure of Mtb OAT globally. Its presence stabilizes the three C-terminal residues that are disordered and not observed in the native structure. Stabilization of the C-terminal residues by ornithine reduces the size of the active-site pocket volume in the structure of the ORN complex. The interactions of ORN and the protein residues of Mtb OAT unambiguously delineate the active-site residues of this enzyme in Mtb. Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.35 ornithine
-
 Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.35 Mycobacterium tuberculosis P9WPZ3
-
-
2.3.1.35 Mycobacterium tuberculosis H37Rv P9WPZ3
-
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.35 Mtb OAT
-
 Mycobacterium tuberculosis