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The human intestinal microbe Bacteroides thetaiotaomicron has an extensive starch utilization system and multiple genesthat are involved in starch binding and utilization. We determined the structure of a xylose isomerase (XI) of Bacteroidesthetaiotaomicron, which belongs to the class 2 XIs. Although the overall structures of XIs from different organisms werehighly similar to each other, some large deviations were found in the class 1 and class 2 XIs; the long N-terminal extensionof class 2 XIs made additional contact with the adjacent subunit of XI, and the C-terminal small α helical domain of XIsexhibited distinguishable structural features between the class 1 and class 2 XIs. However, the structures around the metaland substrate binding site were also almost identical regardless of the XI classes, suggesting common enzymologicalproperties between the class 1 and class 2 XIs.
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참고문헌 (29)
참고문헌 신청
Afonine, P. V. / 2012 / Towards automated crystallographic structure refinement with phenix. refine / Acta Crystallogr D Biol Crystallogr 68:352~367
Asboth, B. / 2000 / Mechanism of action of D-xylose isomerase / Curr Protein Pept Sci 1:237~254
Bhosale, S. H. / 1996 / Molecular cloning and expression of the glucose/xylose isomerase gene from Streptomyces sp. NCIM 2730 in Escherichia coli / FEMS Microbiol Lett 145:95~100
Bhosale, S. H. / 1996 / Molecular and industrial aspects of glucose isomerase / Microbiol Rev 60:280~300
Carrell, H. L. / 1984 / X-ray crystal structure of D-xylose isomerase at 4-A resolution / J Biol Chem 259:3230~3236
Asboth, B. / 2000 / Mechanism of action of D-xylose isomerase / Curr Protein Pept Sci 1:237~254
Bhosale, S. H. / 1996 / Molecular cloning and expression of the glucose/xylose isomerase gene from Streptomyces sp. NCIM 2730 in Escherichia coli / FEMS Microbiol Lett 145:95~100
Bhosale, S. H. / 1996 / Molecular and industrial aspects of glucose isomerase / Microbiol Rev 60:280~300
Carrell, H. L. / 1984 / X-ray crystal structure of D-xylose isomerase at 4-A resolution / J Biol Chem 259:3230~3236
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