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Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from nitrosopumilus maritimus

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dc.contributor.coauthorTolar, Bradley B.
dc.contributor.coauthorDeutsch, Sam
dc.contributor.coauthorYoshikuni, Yasuo
dc.contributor.coauthorWakatsuki, Soichi
dc.contributor.coauthorFrancis, Christopher A.
dc.contributor.departmentDepartment of Molecular Biology and Genetics
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.kuauthorAyan, Esra
dc.contributor.kuauthorDemirci, Hasan
dc.contributor.kuauthorDestan, Ebru
dc.contributor.kuauthorYüksel, Büşra
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.date.accessioned2024-11-09T12:12:08Z
dc.date.issued2021
dc.description.abstractThe ammonia-oxidizing thaumarchaeal 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle is one of the most energy-efficient CO2 fixation cycles discovered thus far. The protein encoded by Nmar_1308 (from Nitrosopumilus maritimus SCM1) is a promiscuous enzyme that catalyzes two essential reactions within the thaumarchaeal 3HP/4HB cycle, functioning as both a crotonyl-CoA hydratase (CCAH) and 3-hydroxypropionyl-CoA dehydratase (3HPD). In performing both hydratase and dehydratase activities, Nmar_1308 reduces the total number of enzymes necessary for CO2 fixation in Thaumarchaeota, reducing the overall cost for biosynthesis. Here, we present the first high-resolution crystal structure of this bifunctional enzyme with key catalytic residues in the thaumarchaeal 3HP/4HB pathway.
dc.description.fulltextYES
dc.description.indexedbyWOS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuTÜBİTAK
dc.description.sponsorshipNational Science Foundation (NSF) Science and Technology Centers
dc.description.sponsorshipScience and Technology Centers
dc.description.sponsorshipScientifc and Technological Research Council of Turkey (TÜBİTAK)
dc.description.sponsorshipUS Department of Energy Joint Genome Institute
dc.description.versionPublisher version
dc.description.volume11
dc.identifier.doi10.1038/s41598-021-02180-8
dc.identifier.embargoNO
dc.identifier.filenameinventorynoIR03349
dc.identifier.issn2045-2322
dc.identifier.quartileQ2
dc.identifier.scopus2-s2.0-85119842220
dc.identifier.urihttps://doi.org/10.1038/s41598-021-02180-8
dc.identifier.wos722365800074
dc.keywordsAmmonia-oxidizing archaea
dc.keywordsNitrifying archaea
dc.keywordsCrystal-Structure
dc.keywordsDiversity
dc.keywordsReveals
dc.keywordsNitrification
dc.keywordsPhysiology
dc.keywordsMechanism
dc.keywordsReductase
dc.keywordsCoenzyme
dc.language.isoeng
dc.publisherNature Portfolio
dc.relation.grantnoNSF-1231306
dc.relation.grantno118C270
dc.relation.grantno119C132
dc.relation.grantnoDE-AC02-05CH11231
dc.relation.grantnoDE-AC02-76SF00515
dc.relation.ispartofScientific Reports
dc.relation.urihttp://cdm21054.contentdm.oclc.org/cdm/ref/collection/IR/id/10135
dc.subjectNitrification
dc.subjectArchaeon
dc.subjectBacteria
dc.titleStructural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from nitrosopumilus maritimus
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.kuauthorDestan, Ebru
local.contributor.kuauthorYüksel, Büşra
local.contributor.kuauthorAyan, Esra
local.contributor.kuauthorDemirci, Hasan
local.publication.orgunit1College of Sciences
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit2Department of Molecular Biology and Genetics
local.publication.orgunit2Graduate School of Sciences and Engineering
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relation.isOrgUnitOfPublication3fc31c89-e803-4eb1-af6b-6258bc42c3d8
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