1QCZ

CRYSTAL STRUCTURE OF E. COLI PURE, AN UNUSUAL MUTASE THAT CATALYZES THE CONVERSION OF N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE (N5-CAIR) TO 4-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE (CAIR) IN THE PURINE BIOSYNTHETIC PATHWAY

Summary for 1QCZ

• Entry DOI: 10.2210/pdb1qcz/pdb
• Descriptor: N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE MUTASE (2 entities in total)
• Functional Keywords: three-layer (alpha-beta-alpha) sandwich, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 17986.85

Authors

Ealick, S.E.,Mathews, I.I. (deposition date: 1999-05-10, release date: 1999-11-10, Last modification date: 2024-10-30)

Primary citation

Mathews, I.I.,Kappock, T.J.,Stubbe, J.,Ealick, S.E.
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway.
Structure Fold.Des., 7:1395-1406, 1999

PubMed Abstract: Conversion of 5-aminoimidazole ribonucleotide (AIR) to 4-carboxyaminoimidazole ribonucleotide (CAIR) in Escherichia coli requires two proteins - PurK and PurE. PurE has recently been shown to be a mutase that catalyzes the unusual rearrangement of N(5)-carboxyaminoimidazole ribonucleotide (N(5)-CAIR), the PurK reaction product, to CAIR. PurEs from higher eukaryotes are homologous to E. coli PurE, but use AIR and CO(2) as substrates to produce CAIR directly.

PubMed: 10574791
DOI: 10.1016/S0969-2126(00)80029-5

Experimental method

X-RAY DIFFRACTION (1.5 Å)