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http://purl.uniprot.org/citations/9843369http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9843369http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9843369http://www.w3.org/2000/01/rdf-schema#comment"Glycinamide ribonucleotide synthetase (GAR-syn) catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi. GAR-syn containing an N-terminal polyhistidine tag was expressed as the SeMet incorporated protein for crystallographic studies. In addition, the protein as isolated contains a Pro294Leu mutation. This protein was crystallized, and the structure solved using multiple-wavelength anomalous diffraction (MAD) phase determination and refined to 1.6 A resolution. GAR-syn adopts an alpha/beta structure that consists of four domains labeled N, A, B, and C. The N, A, and C domains are clustered to form a large central core structure whereas the smaller B domain is extended outward. Two hinge regions, which might readily facilitate interdomain movement, connect the B domain and the main core. A search of structural databases showed that the structure of GAR-syn is similar to D-alanine:D-alanine ligase, biotin carboxylase, and glutathione synthetase, despite low sequence similarity. These four enzymes all utilize similar ATP-dependent catalytic mechanisms even though they catalyze different chemical reactions. Another ATP-binding enzyme with low sequence similarity but unknown function, synapsin Ia, was also found to share high structural similarity with GAR-syn. Interestingly, the GAR-syn N domain shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several dinucleotide-dependent dehydrogenases. Models of ADP and GAR binding were generated based on structure and sequence homology. On the basis of these models, the active site lies in a cleft between the large domain and the extended B domain. Most of the residues that facilitate ATP binding belong to the A or B domains. The N and C domains appear to be largely responsible for substrate specificity. The structure of GAR-syn allows modeling studies of possible channeling complexes with PPRP amidotransferase."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.org/dc/terms/identifier"doi:10.1021/bi981405n"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.org/dc/terms/identifier"doi:10.1021/bi981405n"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Ealick S.E."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Ealick S.E."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Wang W."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Wang W."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Stubbe J."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Stubbe J."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Kappock T.J."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/author"Kappock T.J."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/pages"15647-15662"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/pages"15647-15662"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/title"X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/title"X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/9843369http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/9843369http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9843369
http://purl.uniprot.org/citations/9843369http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9843369
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