1xrc
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CRYSTAL STRUCTURE OF S-ADENOSYLMETHIONINE SYNTHETASE
OverviewOverview
The structure of S-adenosylmethionine synthetase (MAT, ATP:L-methionine, S-adenosyltransferase, EC 2.5.1.6.) from Escherichia coli has been, determined at 3.0 A resolution by multiple isomorphous replacement using a, uranium derivative and the selenomethionine form of the enzyme (SeMAT)., The SeMAT data (9 selenomethionine residues out of 383 amino acid, residues) have been found to have a sufficient phasing power to determine, the structure of the 42,000 molecular weight protein by combining them, with the other heavy atom derivative data (multiple isomorphous, replacement). The enzyme consists of four identical subunits; two subunits, form a spherical tight dimer, and pairs of these dimers form a, peanut-shaped tetrameric enzyme. Each pair dimer has two active sites, which are located between the subunits. Each subunit consists of three, domains that are related to each other by pseudo-3-fold symmetry. The, essential divalent (Mg2+/Co2+) and monovalent (K+) metal ions and one of, the product, Pi ions, were found in the active site from three separate, structures.
About this StructureAbout this Structure
1XRC is a Single protein structure of sequence from Escherichia coli with PO4, CO and K as ligands. Active as Methionine adenosyltransferase, with EC number 2.5.1.6 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of S-adenosylmethionine synthetase., Takusagawa F, Kamitori S, Misaki S, Markham GD, J Biol Chem. 1996 Jan 5;271(1):136-47. PMID:8550549
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