Evidence for major structural changes in the Manduca sexta midgut V(1) ATPase due to redox modulation - A small angle X-ray scattering study

DC FieldValueLanguage
dc.contributor.authorGruber, G
dc.contributor.authorSvergun, DI
dc.contributor.authorGodovac-Zimmermann, J
dc.contributor.authorHarvey, WR
dc.contributor.authorWieczorek, H
dc.contributor.authorKoch, MHJ
dc.date.accessioned2021-12-23T16:23:24Z-
dc.date.available2021-12-23T16:23:24Z-
dc.date.issued2000
dc.identifier.issn00219258
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/14530-
dc.description.abstractThe shape and overall dimensions of the oxidized and reduced form of the V(1) ATPase from Manduca sexta were investigated by synchrotron radiation x-ray solution scattering. The radius of gyration of the oxidized and reduced complex differ noticeably, with dimensions of 6.20 /- 0.06 and 5.84 /- 0.06 nm, respectively, whereas the maximum dimensions remain constant at 22.0 /- 0.1 nm. Comparison of the low resolution shapes of both forms, determined ab initio, indicates that the main structural alteration occurs in the head piece, where the major subunits A and B are located, and at the bottom of the stalk. In conjunction with the solution scattering data, decreased susceptibility to tryptic digestion and tryptophan fluorescence of the reduced V(1) molecule pro vide the first strong evidence for major structural changes in the V(1) ATPase because of redox modulation.
dc.description.sponsorshipNIAID 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; NATIONAL 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
dc.language.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectDISULFIDE BOND FORMATION
dc.subjectELECTRON-MICROSCOPY
dc.subjectMASS-SPECTROMETRY
dc.subjectPROTON PUMP
dc.subjectSUBUNIT-A
dc.subjectSYNCHROTRON RADIATION
dc.subjectTOBACCO HORNWORM MIDGUT
dc.subjectTRANSPORTING PLASMA-MEMBRANES
dc.subjectVACUOLAR H+-ATPASE
dc.subjectVESICLE V-ATPASE
dc.titleEvidence for major structural changes in the Manduca sexta midgut V(1) ATPase due to redox modulation - A small angle X-ray scattering study
dc.typejournal article
dc.identifier.doi10.1074/jbc.M002976200
dc.identifier.isiISI:000089577900024
dc.description.volume275
dc.description.issue39
dc.description.startpage30082
dc.description.endpage30087
dc.contributor.orcid0000-0003-0830-5696
dc.contributor.researcheridE-6863-2010
dc.publisher.place9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatushybrid
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidWiHe990-
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