Open AccessThe structure of an archaeal ribose‐5‐phosphate isomerase from Methanocaldococcus jannaschii (MJ1603)
Author(s) -
Strange Richard W.,
Antonyuk Svetlana V.,
Ellis Mark J.,
Bessho Yoshitaka,
Kuramitsu Seiki,
Yokoyama Shigeyuki,
Hasnain S. Samar
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109044923
Subject(s) - homotetramer , ribose , isomerase , biochemistry , phosphate , enzyme , pentose , chemistry , stereochemistry , biology , protein subunit , fermentation , gene
Ribose‐5‐phosphate isomerase is a ubiquitous intracellular enzyme of bacterial, plant and animal origin that is involved in the pentose phosphate cycle, an essential component of cellular carbohydrate metabolism. Specifically, the enzyme catalyses the reversible conversion of ribose 5‐phosphate to ribulose 5‐phosphate. The structure of ribose‐5‐phosphate isomerase from Methanocaldococcus jannaschii has been solved in space group P 2 1 to 1.78 Å resolution using molecular replacement with one homotetramer in the asymmetric unit and refined to an R factor of 14.8%. The active site in each subunit was occupied by two molecules of propylene glycol in different orientations, one of which corresponds to the location of the phosphate moiety and the other to the location of the furanose ring of the inhibitor.