1CLI

X-RAY CRYSTAL STRUCTURE OF AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE (PURM), FROM THE E. COLI PURINE BIOSYNTHETIC PATHWAY, AT 2.5 A RESOLUTION

Summary for 1CLI

• Entry DOI: 10.2210/pdb1cli/pdb
• Descriptor: PROTEIN (PHOSPHORIBOSYL-AMINOIMIDAZOLE SYNTHETASE), SULFATE ION (3 entities in total)
• Functional Keywords: air synthetase, purm, purine biosynthesis, trifunctional enzyme, purl, fgar amidotransferase, novel fold, ligase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P08178
• Total number of polymer chains: 4
• Total formula weight: 147819.75

Authors

Li, C.,Kappock, T.J.,Stubbe, J.,Weaver, T.M.,Ealick, S.E. (deposition date: 1999-04-28, release date: 1999-10-06, Last modification date: 2023-12-27)

Primary citation

Li, C.,Kappock, T.J.,Stubbe, J.,Weaver, T.M.,Ealick, S.E.
X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.
Structure Fold.Des., 7:1155-1166, 1999

PubMed Abstract: 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).

PubMed: 10508786
DOI: 10.1016/S0969-2126(99)80182-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)