1o92
From Proteopedia
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METHIONINE ADENOSYLTRANSFERASE COMPLEXED WITH ADP AND A L-METHIONINE ANALOGOUS
Overview
Methionine adenosyltransferases (MATs) are a family of enzymes in charge, of synthesising S-adenosylmethionine (SAM), the most important methyl, donor present in living organisms. These enzymes use methionine and ATP as, reaction substrates, which react in a S(N)2 fashion where the sulphur atom, from methionine attacks C5' from ATP while triphosphate chain is cleaved., A MAT liver specific isoenzyme has been detected, which exists in two, distinct oligomeric forms, a dimer (MAT III) and a tetramer (MAT I). Our, previously reported crystal structure of MAT I complexed with an inhibitor, led to the identification of the methionine-binding site. We present here, the results obtained from the complex of MAT I with a competitive, inhibitor of methionine, (2S,4S)-amino-4,5-epoxypentanoic acid ... [(full description)]
About this Structure
1O92 is a [Single protein] structure of sequence from [Rattus norvegicus] with PO4, MG, K, AMB and ADP as [ligands]. Active as [Methionine adenosyltransferase], with EC number [2.5.1.6]. Structure known Active Site: ADP. Full crystallographic information is available from [OCA].
Reference
Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism., Gonzalez B, Pajares MA, Hermoso JA, Guillerm D, Guillerm G, Sanz-Aparicio J, J Mol Biol. 2003 Aug 8;331(2):407-16. PMID:12888348
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