Three-dimensional structure and subunit topology of the V-1 ATPase from Manduca sexta midgut
DC Element | Wert | Sprache |
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dc.contributor.author | Gruber, G | |
dc.contributor.author | Radermacher, M | |
dc.contributor.author | Ruiz, T | |
dc.contributor.author | Godovac-Zimmermann, J | |
dc.contributor.author | Canas, B | |
dc.contributor.author | Kleine-Kohlbrecher, D | |
dc.contributor.author | Huss, M | |
dc.contributor.author | Harvey, WR | |
dc.contributor.author | Wieczorek, H | |
dc.date.accessioned | 2021-12-23T16:21:29Z | - |
dc.date.available | 2021-12-23T16:21:29Z | - |
dc.date.issued | 2000 | |
dc.identifier.issn | 00062960 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13892 | - |
dc.description.abstract | The three-dimensional structure of the Manduca sexta midgut V-1 ATPase has been determined at 3.2 nm resolution from electron micrographs of negatively stained specimens. The V-1 complex has a barrel-like structure Il nm in height and 13.5 nm in diameter. It is hexagonal in the top view, whereas in the side view, the six large subunits A and B are interdigitated for most of their length (9 nm). The topology and importance of the individual subunits of the V-1 complex have been explored by protease digestion, resistance to chaotropic agents, MALDI-TOF mass spectrometry, and CuCl2-induced disulfide formation. Treatment of V-1 with trypsin or chaotropic iodide resulted in a rapid cleavage or release of subunit D from the enzyme, indicating that this subunit is exposed in the complex. Trypsin cleavage of V-1 decreased the ATPase activity with a time course that was in line with the cleavage of subunits B, C, G, and F. When CuCl2 was added to V-1 in the presence of CaADP, the cross-linked products A-E-F and B-H were generated. In experiments where CuCl2 was added after preincubation of CaATP, the cross-linked products E-F and E-G were formed. These changes in cross-linking of subunit E to near-neighbor subunits support the hypothesis that these are nucleotide-dependent conformational changes of the E subunit. | |
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 | 3-DIMENSIONAL RECONSTRUCTION | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | CRYOELECTRON MICROSCOPY | |
dc.subject | ELECTRON-MICROSCOPY | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | F1 ADENOSINE-TRIPHOSPHATASE | |
dc.subject | GAMMA-SUBUNIT | |
dc.subject | MOLECULAR ARCHITECTURE | |
dc.subject | TOBACCO HORNWORM MIDGUT | |
dc.subject | V-TYPE ATPASE | |
dc.subject | VACUOLAR-TYPE ATPASE | |
dc.title | Three-dimensional structure and subunit topology of the V-1 ATPase from Manduca sexta midgut | |
dc.type | journal article | |
dc.identifier.doi | 10.1021/bi000103u | |
dc.identifier.isi | ISI:000088376900029 | |
dc.description.volume | 39 | |
dc.description.issue | 29 | |
dc.description.startpage | 8609 | |
dc.description.endpage | 8616 | |
dc.contributor.researcherid | E-6863-2010 | |
dc.contributor.researcherid | O-9256-2019 | |
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.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | HuMa001 | - |
crisitem.author.netid | WiHe990 | - |
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geprüft am 06.06.2024