1bhj
From Proteopedia
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CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)
Overview
The crystal structure of the recombinant apo-form of glycine, N-methyltransferase (GNMT) has been determined at 2.5 A resolution. GNMT, is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that, catalyzes the transfer of a methyl group from S-adenosylmethionine, (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy), and sarcosine (N-methylglycine). GNMT is a regulatory enzyme, which is, inhibited by 5-methyltetrahydrofolate pentaglutamate and believed to, control the ratio of AdoMet to AdoHcy in tissues. The crystals belong to, the orthorhombic space group P2(1)2(1)2 (a = 85.39, b = 174.21, c = 44.71, A) and contain one dimer per asymmetric unit. The AdoMet-GNMT structure, served as the starting model. The structure was refined to an R-factor of, 21.9%. Each monomer is a three-domain structure with a large cavity, enclosed by the three domains. The tetramer resembles a square with a, central channel about which N-terminal domains are intertwined. Only, localized changes of the residues involved in the binding pocket are, observed for the apo-GNMT structure when compared to that determined in, the presence of substrate and substrate analog.
About this Structure
1BHJ is a Single protein structure of sequence from Rattus norvegicus. Active as Glycine N-methyltransferase, with EC number 2.1.1.20 Full crystallographic information is available from OCA.
Reference
Crystal structure of apo-glycine N-methyltransferase (GNMT)., Pattanayek R, Newcomer ME, Wagner C, Protein Sci. 1998 Jun;7(6):1326-31. PMID:9655336
Page seeded by OCA on Tue Nov 20 11:39:43 2007
