1o92

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Revision as of 19:22, 29 October 2007

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spinqualitylabelsall models 1o92, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [[1]], with EC number [2.5.1.6]. 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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