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.
Swan
Michael K
MK
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston 29425, USA.
Hansen
Thomas
T
Schönheit
Peter
P
Davies
Christopher
C
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