2CAN

HUMAN ORNITHINE AMINOTRANSFERASE COMPLEXED WITH L-CANALINE

Summary for 2CAN

• Entry DOI: 10.2210/pdb2can/pdb
• Descriptor: ORNITHINE AMINOTRANSFERASE, CANALINE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase, ornithine aminotransferase, urea cycle, pyridoxal-5'-phosphate
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: P04181
• Total number of polymer chains: 3
• Total formula weight: 135262.30

Authors

Shah, S.A.,Shen, B.W.,Brunger, A.T. (deposition date: 1997-05-29, release date: 1998-06-03, Last modification date: 2024-05-22)

Primary citation

Shah, S.A.,Shen, B.W.,Brunger, A.T.
Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition.
Structure, 5:1067-1075, 1997

PubMed Abstract: Ornithine aminotransferase (OAT) is a 45 kDa pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes the conversion of L-ornithine and 2-oxoglutarate to glutamate-delta-semialdehyde and glutamic acid, respectively. In humans, loss of OAT function causes an accumulation of ornithine that results in gyrate atrophy of the choroid and retina, a disease that progressively leads to blindness. In an effort to learn more about the structural basis of this enzyme's function, we have determined the X-ray structures of OAT in complex with two enzyme-activated suicide substrates: L-canaline, an ornithine analog, and gabaculine, an irreversible inhibitor of several related aminotransferases.

PubMed: 9309222
DOI: 10.1016/S0969-2126(97)00258-X

Experimental method

X-RAY DIFFRACTION (2.3 Å)