Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography
dc.authorid | Demirci, Hasan/0000-0002-9135-5397 | |
dc.authorid | Gul, Mehmet/0000-0001-5513-1866 | |
dc.authorwosid | Demirci, Hasan/HJP-7731-2023 | |
dc.contributor.author | Gul, Mehmet | |
dc.contributor.author | Yuksel, Busra | |
dc.contributor.author | Bulut, Huri | |
dc.contributor.author | DeMirci, Hasan | |
dc.date.accessioned | 2024-05-19T14:41:38Z | |
dc.date.available | 2024-05-19T14:41:38Z | |
dc.date.issued | 2023 | |
dc.department | İstinye Üniversitesi | en_US |
dc.description.abstract | Candida boidinii NAD(+)- dependent formate dehydrogenase (CbFDH) has gained significant attention for its potential application in the production of biofuels and various industrial chemicals from inorganic carbon dioxide. The present study reports the atomic X-ray crystal structures of wild-type CbFDH at cryogenic and ambient temperatures, as well as that of the Val120Thr mutant at cryogenic temperature, determined at the Turkish Light Source 'Turkish DeLight'. The structures reveal new hydrogen bonds between Thr120 and water molecules in the active site of the mutant CbFDH, suggesting increased stability of the active site and more efficient electron transfer during the reaction. Further experimental data is needed to test these hypotheses. Collectively, these findings provide invaluable insights into future protein-engineering efforts that could potentially enhance the efficiency and effectiveness of CbFDH. | en_US |
dc.description.sponsorship | NSF Science and Technology Center grant [NSF-1231306]; 2232 International Fellowship for Outstanding Researchers Program of TUBITAK [118C270]; TUBITAK | en_US |
dc.description.sponsorship | HD acknowledges support from NSF Science and Technology Center grant NSF-1231306 (Biology with X-ray Lasers, BioXFEL). This publication has been produced benefiting from the 2232 International Fellowship for Outstanding Researchers Program of TUBITAK (Project No. 118C270). However, the entire responsibility for the publication belongs to the authors of the publication. The financial support received from TUBITAK does not mean that the content of the publication is approved in a scientific sense by TUBITAK. | en_US |
dc.identifier.doi | 10.1107/S2059798323008070 | |
dc.identifier.endpage | 1017 | en_US |
dc.identifier.issn | 2059-7983 | |
dc.identifier.pmid | 37860962 | en_US |
dc.identifier.scopus | 2-s2.0-85175742206 | en_US |
dc.identifier.scopusquality | Q1 | en_US |
dc.identifier.startpage | 1010 | en_US |
dc.identifier.uri | https://doi.org10.1107/S2059798323008070 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12713/5137 | |
dc.identifier.volume | 79 | en_US |
dc.identifier.wos | WOS:001098067400005 | en_US |
dc.identifier.wosquality | N/A | en_US |
dc.indekslendigikaynak | Web of Science | en_US |
dc.indekslendigikaynak | Scopus | en_US |
dc.language.iso | en | en_US |
dc.publisher | Int Union Crystallography | en_US |
dc.relation.ispartof | Acta Crystallographica Section D-Structural Biology | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.snmz | 20240519_ka | en_US |
dc.subject | Formate Dehydrogenases | en_US |
dc.subject | Candida Boidinii | en_US |
dc.subject | Protein Engineering | en_US |
dc.subject | X-Ray Crystallography | en_US |
dc.subject | Structural Biology | en_US |
dc.subject | Structural Dynamics | en_US |
dc.subject | Turkish Light Source | en_US |
dc.subject | Turkish Delight | en_US |
dc.title | Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography | en_US |
dc.type | Article | en_US |