Crystallization and preliminary X-ray diffraction analysis of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum.
Phosphoglucose isomerase from the crenarchaeon Pyrobaculum aerophilum (PaPGI/PMI) shows virtually no sequence similarity to its counterparts from bacterial and eukaryotic sources and belongs to a unique group within the PGI superfamily. Whereas conventional PGIs show strict substrate specificity for glucose 6-phosphate and fructose 6-phosphate, PaPGI/PMI can also catalyse the isomerization of mannose 6-phosphate. In order to establish its relatedness within the PGI family and to elucidate the structural basis for its broader specificity, this enzyme was crystallized. The crystals belong to space group P2(1) and a complete data set extending to 1.6 A resolution has been collected.
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston 29425, USA.
Michael K
MK
Swan
Thomas
T
Hansen
Peter
P
Schönheit
Christopher
C
Davies
D000595:Amino Acid Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D008359:Mannose-6-Phosphate Isomerase / Q000737:chemistry*; D008969:Molecular Sequence Data; D041543:Pyrobaculum / Q000201:enzymology*
D008359:Mannose-6-Phosphate Isomerase