2v9y
From Proteopedia
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HUMAN AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE
Overview
BACKGROUND: The purine biosynthetic pathway in procaryotes enlists eleven, enzymes, six of which use ATP. Enzymes 5 and 6 of this pathway, formylglycinamide ribonucleotide (FGAR) amidotransferase (PurL) and, aminoimidazole ribonucleotide (AIR) synthetase (PurM) utilize ATP to, activate the oxygen of an amide within their substrate toward nucleophilic, attack by a nitrogen. AIR synthetase uses the product of PurL, formylglycinamidine ribonucleotide (FGAM) and ATP to make AIR, ADP and, P(i). RESULTS: The structure of a hexahistidine-tagged PurM has been, solved by multiwavelength anomalous diffraction phasing techniques using, protein containing 28 selenomethionines per asymmetric unit. The final, model of PurM consists of two crystallographically independent dimers and, four sulfates. The ... [(full description)]
About this Structure
2V9Y is a [Single protein] structure of sequence from [Homo sapiens] with SO4 as [ligand]. Active as [[1]], with EC number [6.3.3.1]. Full crystallographic information is available from [OCA].
Reference
X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution., Li C, Kappock TJ, Stubbe J, Weaver TM, Ealick SE, Structure. 1999 Sep 15;7(9):1155-66. PMID:10508786
Page seeded by OCA on Mon Oct 29 23:04:32 2007
Categories: Homo sapiens | Single protein | Arrowsmith, C.H. | Berg, S.Van.Den. | Berglund, H. | Busam, R. | Collins, R. | Consortium, Structural.Genomics. | Dahlgren, L.G. | Edwards, A. | Flodin, S. | Flores, A. | Graslund, S. | Hallberg, B.M. | Hammarstrom, M. | Herman, M.D. | Holmberg-Schiavone, L. | Johansson, I. | Kallas, A. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nordlund, P. | Nyman, T. | Persson, C. | Sagemark, J. | Stenmark, P. | Sundstrom, M. | Thorsell, A.G. | Tresaugues, L. | Weigelt, J. | Welin, M. | SO4 | Airs | Alternative splicing | Aminoimidazole ribonucleotide synthetase | Atp-binding | Gart | Ligase | Multifunctional enzyme | Nucleotide-binding | Phosphorylation | Polymorphism | Purine biosynthesis | Purine metabolism | Sgc | Structural genomics | Structural genomics consortium | Transferase