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
Protein & Peptide Letters
Title: Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus
Volume: 10 Issue: 5
Author(s): Michael K. Swan, Thomas Hansen, Peter Schonheit and Christopher Davies
Affiliation:
Keywords: pyrococcus furiosus, phosphoglucose isomerase, cupin fold, x-ray crystallography
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.
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Cite this article as:
Swan K. Michael, Hansen Thomas, Schonheit Peter and Davies Christopher, Crystallization And Preliminary X-Ray Diffraction Analysis Of Phosphoglucose Isomerase From Pyrococcus Furiosus, Protein & Peptide Letters 2003; 10 (5) . https://dx.doi.org/10.2174/0929866033478762
DOI https://dx.doi.org/10.2174/0929866033478762 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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