Structure-function relationships of A-, F- and V-ATPases

DC FieldValueLanguage
dc.contributor.authorGruber, G
dc.contributor.authorWieczorek, H
dc.contributor.authorHarvey, WR
dc.contributor.authorMuller, V
dc.date.accessioned2021-12-23T16:21:04Z-
dc.date.available2021-12-23T16:21:04Z-
dc.date.issued2001
dc.identifier.issn00220949
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/13714-
dc.description.abstractIon-translocating ATPases, such as the F1Fo-, V1Vo- and archaeal A(1)A(o) enzymes, are essential cellular energy converters which transduce the chemical energy of ATP hydrolysis into transmembrane ionic electrochemical potential differences. Based on subunit composition and primary structures of the subunits, these types of ATPases are related through evolution; however, they differ with respect to function. Recent work has focused on the three-dimensional structural relationships of the major, nucleotide-binding subunits A and B of the A(1)/V-1-ATPases and the corresponding beta and alpha subunits of the F-1-ATPase, and the location of the coupling subunits within the stalk that provide the physical linkage between the regions of ATP hydrolysis and ion transduction. This review focuses on the structural homologies and diversities of A(1)-, F-1- and V-1-ATPases, in particular on significant differences between the stalk regions of these families of enzymes.
dc.description.sponsorshipNATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R01AI022444] Funding Source: NIH RePORTER; NIAID NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [AI 22444] Funding Source: Medline
dc.language.isoen
dc.publisherCOMPANY OF BIOLOGISTS LTD
dc.relation.ispartofJOURNAL OF EXPERIMENTAL BIOLOGY
dc.subjectA(1)A(o)-ATPase
dc.subjectarchaea-type ATPase
dc.subjectBiology
dc.subjectC-SUBUNIT OLIGOMER
dc.subjectCLATHRIN-COATED VESICLE
dc.subjectCOLI ATP SYNTHASE
dc.subjectDELTA-SUBUNIT
dc.subjectELECTRON-MICROSCOPY
dc.subjectEPSILON-SUBUNIT
dc.subjectEscherichia coli
dc.subjectESCHERICHIA-COLI
dc.subjectF1Fo-ATPase
dc.subjectGAMMA-SUBUNIT
dc.subjectH+ translocating vacuolar-type ATPase
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectManduca sexta
dc.subjectMANDUCA-SEXTA MIDGUT
dc.subjectMethanosarcina mazei
dc.subjectsmall-angle X-ray scattering
dc.subjectV-1-ATPase
dc.subjectVACUOLAR H+-ATPASE
dc.titleStructure-function relationships of A-, F- and V-ATPases
dc.typereview
dc.identifier.isiISI:000170563500001
dc.description.volume204
dc.description.issue15
dc.description.startpage2597
dc.description.endpage2605
dc.contributor.orcid0000-0001-7955-5508
dc.contributor.researcheridABE-4305-2021
dc.publisher.placeBIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND
dcterms.isPartOf.abbreviationJ. Exp. Biol.
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidWiHe990-
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