Literature summary for 2.3.1.35 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Inhibitors	Comment	Organism	Structure
ornithine	-	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WPZ3	-	-
Mycobacterium tuberculosis H37Rv	P9WPZ3	-	-

Synonyms

Synonyms	Comment	Organism
Mtb OAT	-	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)