Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor
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 previ...
| 发表在: | Data in Brief |
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| Main Authors: | , |
| 格式: | 文件 |
| 语言: | 英语 |
| 出版: |
Elsevier
2024-02-01
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| 主题: | |
| 在线阅读: | http://www.sciencedirect.com/science/article/pii/S2352340923009551 |
| _version_ | 1851846713720963072 |
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| author | Yongbin Xu Ki Hyun Nam |
| author_facet | Yongbin Xu Ki Hyun Nam |
| author_sort | Yongbin Xu |
| collection | DOAJ |
| container_title | Data in Brief |
| description | 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 Streptomyces rubiginosus 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. |
| format | Article |
| id | doaj-art-e9f818b937cd477b90541502b2c82297 |
| institution | Directory of Open Access Journals |
| issn | 2352-3409 |
| language | English |
| publishDate | 2024-02-01 |
| publisher | Elsevier |
| record_format | Article |
| spelling | doaj-art-e9f818b937cd477b90541502b2c822972025-08-19T22:26:04ZengElsevierData in Brief2352-34092024-02-015210991610.1016/j.dib.2023.109916Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitorYongbin Xu0Ki Hyun Nam1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, China; Key Laboratory of Biotechnology and Bioresources Utilization of Ministry of Education, College of Life Science, Dalian Minzu University, Dalian 116600, ChinaCollege of General Education, Kookmin University, Seoul 02707, South Korea; Corresponding author.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 Streptomyces rubiginosus 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.http://www.sciencedirect.com/science/article/pii/S2352340923009551Glucose isomeraseX-ray crystallographySubatomic resolutionData collectionRadiation damageData processing |
| spellingShingle | Yongbin Xu Ki Hyun Nam Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor Glucose isomerase X-ray crystallography Subatomic resolution Data collection Radiation damage Data processing |
| title | Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| title_full | Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| title_fullStr | Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| title_full_unstemmed | Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| title_short | Data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| title_sort | data of the subatomic resolution structure of glucose isomerase complexed with xylitol inhibitor |
| topic | Glucose isomerase X-ray crystallography Subatomic resolution Data collection Radiation damage Data processing |
| url | http://www.sciencedirect.com/science/article/pii/S2352340923009551 |
| work_keys_str_mv | AT yongbinxu dataofthesubatomicresolutionstructureofglucoseisomerasecomplexedwithxylitolinhibitor AT kihyunnam dataofthesubatomicresolutionstructureofglucoseisomerasecomplexedwithxylitolinhibitor |
