The structure of an archaeal ribose-5-phosphate isomerase from Methanocaldococcus jannaschii (MJ1603).
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 P2(1) to 1.78 A 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.
Strange
Richard W
RW
Molecular Biophysics Group, School of Biological Sciences, University of Liverpool, Crown Street, Liverpool L69 7ZB, England. r.strange@liverpool.ac.uk
Antonyuk
Svetlana V
SV
Ellis
Mark J
MJ
Bessho
Yoshitaka
Y
Kuramitsu
Seiki
S
Yokoyama
Shigeyuki
S
Hasnain
S Samar
SS
D019747:Aldose-Ketose Isomerases / Q000737:chemistry* / Q000235:genetics; D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D019766:Genes, Archaeal; D017015:Methanococcales / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D019946:Propylene Glycol / Q000737:chemistry; D017510:Protein Folding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D055672:Static Electricity
D021122:Protein Subunits; D011994:Recombinant Proteins; D019946:Propylene Glycol; D019747:Aldose-Ketose Isomerases; C022548:ribosephosphate isomerase