Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus

Authors: Swan M.K.; Hansen T.; Schonheit P.; Davies C.

Source: Protein and Peptide Letters, Volume 10, Number 5, October 2003 , pp. 517-520(4)

Publisher: Bentham Science Publishers

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Abstract:

In several euryarchaeota, phosphoglucose isomerase (PGI) activity is catalyzed by an enzyme unrelated to the well-known family of PGI enzymes found in prokaryotes, eukaryotes and some archaea. In order to understand the mechanistic differences between the two families of enzymes we have crystallized PGI from the archaeon Pyrococcus furiosus. The crystals belong to the space group P21 and a complete dataset extending to 1.9 Å resolution has been collected.

Keywords: pyrococcus furiosus; phosphoglucose isomerase; cupin fold; x-ray crystallography

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866033478762

Affiliations: 1: Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425 USA.

Publication date: 2003-10-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.