Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities

DC FieldValueLanguage
dc.contributor.authorSvergun, DI
dc.contributor.authorKonrad, S
dc.contributor.authorHuss, M
dc.contributor.authorKoch, MHJ
dc.contributor.authorWieczorek, H
dc.contributor.authorAltendorf, K
dc.contributor.authorVolkov, VV
dc.contributor.authorGruber, G
dc.date.accessioned2021-12-23T16:17:10Z-
dc.date.available2021-12-23T16:17:10Z-
dc.date.issued1998
dc.identifier.issn00062960
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/12238-
dc.description.abstractThe V-1 ATPase from the tobacco hornworm Manduca sexta and the Escherichia coli F-1 ATPase were characterized by small-angle X-ray scattering (SAXS). The radii of gyration (R-g) of the complexes were 6.2 /- 0.1 and 4.7 /- 0.02 nm, respectively. The shape of the M. sexta V-1 ATPase was determined ab initio from the scattering data showing six masses, presumed to be the A and B subunits, arranged in an alternating manner about a 3-fold axis. A seventh mass with a length of about 11.0 nm extends perpendicularly to the center of the hexameric unit. This central mass is presumed to be the stalk that connects V-1 with the membrane domain (V-o) in the intact V1Vo-ATPase. In comparison, the shape of the F-1 ATPase from E. coli possesses a quasi-3-fold symmetry over the major part of the enzyme. The overall asymmetry of the structure is given by a stem, assumed to include the central stalk subunits. The features of the V-1 and F-1 ATPase reveal structural homologies and diversities of the key components of the complexes.
dc.description.sponsorshipPHS HHSUnited States Department of Health & Human ServicesUnited States Public Health Service [A1 22444] Funding Source: Medline
dc.language.isoen
dc.publisherAMER CHEMICAL SOC
dc.relation.ispartofBIOCHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectDIRECT SHAPE DETERMINATION
dc.subjectKDA SUBUNIT
dc.subjectMEMBRANE
dc.subjectNEUROSPORA-CRASSA
dc.subjectPURIFICATION
dc.subjectSMALL-ANGLE-SCATTERING
dc.subjectSYNCHROTRON RADIATION
dc.subjectTOBACCO HORNWORM MIDGUT
dc.subjectV-ATPASE
dc.subjectVACUOLAR H+-ATPASE
dc.titleQuaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities
dc.typejournal article
dc.identifier.doi10.1021/bi982367a
dc.identifier.isiISI:000077848400004
dc.description.volume37
dc.description.issue51
dc.description.startpage17659
dc.description.endpage17663
dc.contributor.orcid0000-0003-0830-5696
dc.publisher.place1155 16TH ST, NW, WASHINGTON, DC 20036 USA
dcterms.isPartOf.abbreviationBiochemistry
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidHuMa001-
crisitem.author.netidWiHe990-
crisitem.author.netidAlKa770-
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