Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor.
Data Brief
College of General Education, Kookmin University, Seoul 02707, South Korea.
Published: February 2024
Glucose isomerase (GI) is a crucial enzyme in industrial processes, including the production of high-fructose corn syrup, biofuels, and other renewable chemicals. Understanding the mechanisms of GI inhibition by GI inhibitors can offer valuable insights into enhancing production efficiency. We previously reported the subatomic resolution structure of GI (SruGI) complexed with a xylitol inhibitor, determined at 0.99 Å resolution, was reported. Structural analysis showed that the xylitol inhibitor is partially bound to the M1 binding site at the SruGI active site, enabling it to distinguish the xylitol-bound and -free state of SruGI. This structural information demonstrates that xylitol binding to the M1 site causes a conformational change in the metal binding site and the substrate binding channel of SruGI. Herein, detailed information on data collection and processing procedures of the subatomic resolution structure of the SruGI complexed with xylitol was reported.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10792680 | PMC |
| http://dx.doi.org/10.1016/j.dib.2023.109916 | DOI Listing |
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