2018
Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites
Mnatsakanyan N, Li Y, Weber J. Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites. Journal Of Biological Chemistry 2018, 294: 1152-1160. PMID: 30510135, PMCID: PMC6349107, DOI: 10.1074/jbc.ra118.002504.Peer-Reviewed Original ResearchATP Synthetase ComplexesBinding SitesBiocatalysisGeobacillus stearothermophilusNucleotidesProtein Subunits
2011
The β Subunit Loop That Couples Catalysis and Rotation in ATP Synthase Has a Critical Length*
Mnatsakanyan N, Kemboi SK, Salas J, Weber J. The β Subunit Loop That Couples Catalysis and Rotation in ATP Synthase Has a Critical Length*. Journal Of Biological Chemistry 2011, 286: 29788-29796. PMID: 21705326, PMCID: PMC3191020, DOI: 10.1074/jbc.m111.254730.Peer-Reviewed Original Research
2009
The Role of the βDELSEED-loop of ATP Synthase*
Mnatsakanyan N, Krishnakumar AM, Suzuki T, Weber J. The Role of the βDELSEED-loop of ATP Synthase*. Journal Of Biological Chemistry 2009, 284: 11336-11345. PMID: 19246448, PMCID: PMC2670139, DOI: 10.1074/jbc.m900374200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceATP Synthetase ComplexesBacillusBinding SitesCell MembraneEscherichia coliMitochondrial Proton-Translocating ATPasesMolecular ConformationMolecular Sequence DataMutationNucleotidesPhosphorylationProtein Structure, TertiarySequence Homology, Amino AcidConceptsWild-type enzymeATP synthaseDELSEED-loopDeletion mutantsATP hydrolysisUnique rotational mechanismTransmembrane proton gradientHelix motifRate-limiting catalytic stepTerminal domainFunctional analysisMutantsBeta subunitMembrane vesiclesATP synthesisProton gradientAmino acidsLow abundanceCatalytic stepMechanochemical couplingCatalytic siteSynthaseChemical energyEnzymeMembrane preparations