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1ajs
From Proteopedia
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Revision as of 12:44, 30 October 2007
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REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE
Overview
Two high resolution crystal structures of cytosolic aspartate, aminotransferase from pig heart provide additional insights into the, stereochemical mechanism for ligand-induced conformational changes in this, enzyme. Structures of the homodimeric native structure and its complex, with the substrate analog 2-methylaspartate have been refined, respectively, with 1.74-A x-ray diffraction data to an R value of 0.170, and with 1.6-A data to an R value of 0.173. In the presence of, 2-methylaspartate, one of the subunits (subunit 1) shows a ligand-induced, conformational change that involves a large movement of the small domain, (residues 12-49 and 327-412) to produce a "closed" conformation. No such, transition is observed in the other subunit (subunit 2), because crystal, lattice contacts lock ... [(full description)]
About this Structure
1AJS is a [Protein complex] structure of sequences from [Sus scrofa] with PLA as [ligand]. Active as [Aspartate transaminase], with EC number [2.6.1.1]. Structure known Active Sites: ACT and AXT. Full crystallographic information is available from [OCA].
Reference
Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate., Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A, J Biol Chem. 1997 Jul 11;272(28):17293-302. PMID:9211866
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