Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Svergun, DI | |
dc.contributor.author | Konrad, S | |
dc.contributor.author | Huss, M | |
dc.contributor.author | Koch, MHJ | |
dc.contributor.author | Wieczorek, H | |
dc.contributor.author | Altendorf, K | |
dc.contributor.author | Volkov, VV | |
dc.contributor.author | Gruber, G | |
dc.date.accessioned | 2021-12-23T16:17:10Z | - |
dc.date.available | 2021-12-23T16:17:10Z | - |
dc.date.issued | 1998 | |
dc.identifier.issn | 00062960 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/12238 | - |
dc.description.abstract | The 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.sponsorship | PHS HHSUnited States Department of Health & Human ServicesUnited States Public Health Service [A1 22444] Funding Source: Medline | |
dc.language.iso | en | |
dc.publisher | AMER CHEMICAL SOC | |
dc.relation.ispartof | BIOCHEMISTRY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | DIRECT SHAPE DETERMINATION | |
dc.subject | KDA SUBUNIT | |
dc.subject | MEMBRANE | |
dc.subject | NEUROSPORA-CRASSA | |
dc.subject | PURIFICATION | |
dc.subject | SMALL-ANGLE-SCATTERING | |
dc.subject | SYNCHROTRON RADIATION | |
dc.subject | TOBACCO HORNWORM MIDGUT | |
dc.subject | V-ATPASE | |
dc.subject | VACUOLAR H+-ATPASE | |
dc.title | Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities | |
dc.type | journal article | |
dc.identifier.doi | 10.1021/bi982367a | |
dc.identifier.isi | ISI:000077848400004 | |
dc.description.volume | 37 | |
dc.description.issue | 51 | |
dc.description.startpage | 17659 | |
dc.description.endpage | 17663 | |
dc.contributor.orcid | 0000-0003-0830-5696 | |
dc.publisher.place | 1155 16TH ST, NW, WASHINGTON, DC 20036 USA | |
dcterms.isPartOf.abbreviation | Biochemistry | |
crisitem.author.dept | Universität Osnabrück | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | HuMa001 | - |
crisitem.author.netid | WiHe990 | - |
crisitem.author.netid | AlKa770 | - |
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