Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 Å resolution

Eric L. Wise, Julie Akana, John A. Gerlt, Ivan Rayment

Research output: Contribution to journalArticlepeer-review

Abstract

The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 Å resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (β/α)8-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues.

Original languageEnglish (US)
Pages (from-to)1687-1690
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number9
DOIs
StatePublished - Sep 2004

ASJC Scopus subject areas

  • Structural Biology

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