1grc
From Proteopedia
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CRYSTAL STRUCTURE OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE FROM ESCHERICHIA COLI AT 3.0 ANGSTROMS RESOLUTION: A TARGET ENZYME FOR CHEMOTHERAPY
Overview
The atomic structure of glycinamide ribonucleotide transformylase, an, essential enzyme in purine biosynthesis, has been determined at 3.0 A, resolution. The last three C-terminal residues and a sequence stretch of, 18 residues (residues 113 to 130) are not visible in the electron density, map. The enzyme forms a dimer in the crystal structure. Each monomer is, divided into two domains, which are connected by a central mainly parallel, seven-stranded beta-sheet. The N-terminal domain contains a Rossmann type, mononucleotide fold with a phosphate ion bound to the C-terminal end of, the first beta-strand. A long narrow cleft stretches from the phosphate to, a conserved aspartic acid, Asp144, which has been suggested as an, active-site residue. The cleft is lined by a cluster of residues, which, are conserved between bacterial, yeast, avian and human enzymes, and, likely represents the binding pocket and active site of the enzyme. GAR, Tfase binds a reduced folate cofactor and glycinamide ribonucleotide for, the catalysis of one of the initial steps in purine biosynthesis. Folate, analogs and multi-substrate inhibitors of the enzyme have antineoplastic, effects and the structure determination of the unliganded enzyme and, enzyme-inhibitor complexes will aid the development of anti-cancer drugs.
About this Structure
1GRC is a Single protein structure of sequence from Escherichia coli with PO4 as ligand. Active as Phosphoribosylglycinamide formyltransferase, with EC number 2.1.2.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution. A target enzyme for chemotherapy., Chen P, Schulze-Gahmen U, Stura EA, Inglese J, Johnson DL, Marolewski A, Benkovic SJ, Wilson IA, J Mol Biol. 1992 Sep 5;227(1):283-92. PMID:1522592
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