1bjo
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(New page: 200px<br /> <applet load="1bjo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bjo, resolution 2.80Å" /> '''THE STRUCTURE OF PH...)
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Revision as of 18:12, 29 October 2007
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THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE
Overview
Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup, IV of the aminotransferases, catalyses the conversion of, 3-phosphohydroxypyruvate to l-phosphoserine. The crystal structure of PSAT, from Escherichia coli has been solved in space group P212121 using MIRAS, phases in combination with density modification and was refined to an, R-factor of 17.5% (Rfree=20.1 %) at 2.3 A resolution. In addition, the, structure of PSAT in complex with alpha-methyl-l-glutamate (AMG) has been, refined to an R-factor of 18.5% (Rfree=25.1%) at 2.8 A resolution. Each, subunit (361 residues) of the PSAT homodimer is composed of a large, pyridoxal-5'-phosphate binding domain (residues 16-268), consisting of a, seven-stranded mainly parallel beta-sheet, two additional beta-strands and, seven ... [(full description)]
About this Structure
1BJO is a [Single protein] structure of sequence from [Escherichia coli] with PLP as [ligand]. Active as [[1]], with EC number [2.6.1.52]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate., Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN, J Mol Biol. 1999 Feb 26;286(3):829-50. PMID:10024454
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