1D7A

CRYSTAL STRUCTURE OF E. COLI PURE-MONONUCLEOTIDE COMPLEX.

Summary for 1D7A

• Entry DOI: 10.2210/pdb1d7a/pdb
• Related: 1QCZ
• Descriptor: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE, 5-AMINOIMIDAZOLE RIBONUCLEOTIDE (3 entities in total)
• Functional Keywords: three-layer (alpha-beta-alpha) sandwich n5-cair mutase (pure), aminoimidazole ribonucleotide (air), lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 138091.74

Authors

Mathews, I.I.,Kappock, T.J.,Stubbe, J.,Ealick, S.E. (deposition date: 1999-10-16, release date: 1999-12-03, Last modification date: 2024-11-20)

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 (2.5 Å)