Overexpression, crystallization and preliminary X‐ray crystallographic analysis of d‐ribose‐5‐phosphate isomerase from Clostridium thermocellum
Publisher：
John Wiley & Sons Inc
E-ISSN：
1744-3091|65|11|1141-1144
ISSN：
1744-3091
Source：
Acta Crystallographica Section F,
Vol.65,
Iss.11, 2009-11,
pp. : 1141-1144
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Abstract
Rare sugars are used for many industrial and medical purposes and are produced by the interconversion between aldoses and ketoses catalyzed by sugar and sugar‐phosphate isomerases. Recently, Clostridium thermocellumd‐ribose‐5‐phosphate isomerase (CTRPI), an aldose–ketose isomerase, was cloned in order to synthesize d‐allose and its substrate specificity was further characterized for industrial usage. CTRPI has a novel substrate specificity that differs from those of other isomerases, which have broad substrate specificities. CTRPI prefers aldose substrates such as l‐talose, d‐ribose and d‐allose. CTRPI was purified and crystallized in order to determine its three‐dimensional structure and thus to elucidate its enzymatic reaction mechanism and understand its substrate specificity. The crystal belonged to the trigonal space group P3221, with unit‐cell parameters a = b = 69.5, c = 154.4 Å, and diffracted to 1.9 Å resolution. According to Matthews coefficient calculations, the crystallographic structure consists of a dimer in the asymmetric unit, with a VM of 3.2 Å3 Da−1 and a solvent content of 61.7%.
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