Publication:
Structural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography

dc.contributor.coauthorYuksel, Busra
dc.contributor.coauthorBulut, Huri
dc.contributor.departmentDepartment of Molecular Biology and Genetics
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.kuauthorGül, Mehmet
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.date.accessioned2025-01-19T10:31:12Z
dc.date.issued2023
dc.description.abstractCandida 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.
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.openaccessGreen Submitted, Green Published, hybrid
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.description.sponsorshipHD 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.
dc.description.volume79
dc.identifier.doi10.1107/S2059798323008070
dc.identifier.issn2059-7983
dc.identifier.quartileQ1
dc.identifier.scopus2-s2.0-85175742206
dc.identifier.urihttps://doi.org/10.1107/S2059798323008070
dc.identifier.urihttps://hdl.handle.net/20.500.14288/26182
dc.identifier.wos1098067400005
dc.keywordsFormate dehydrogenases
dc.keywordsCandida boidinii
dc.keywordsProtein engineering
dc.keywordsX-ray crystallography
dc.keywordsStructural biology
dc.keywordsStructural dynamics
dc.keywordsTurkish light source
dc.language.isoeng
dc.publisherInt Union Crystallography
dc.relation.grantnoNSF Science and Technology Center grant [NSF-1231306]; 2232 International Fellowship for Outstanding Researchers Program of TUBITAK [118C270]; TUBITAK
dc.relation.ispartofActa Crystallographica Section D-Structural Biology
dc.subjectBiochemistry and molecular biology
dc.subjectBiophysics
dc.subjectCrystallography
dc.titleStructural analysis of wild-type and Val120Thr mutant Candida boidinii formate dehydrogenase by X-ray crystallography
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorGül, Mehmet
local.contributor.kuauthorDemirci Hasan
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit1College of Sciences
local.publication.orgunit2Department of Molecular Biology and Genetics
local.publication.orgunit2Graduate School of Sciences and Engineering
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