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http://purl.uniprot.org/citations/12626496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12626496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12626496http://www.w3.org/2000/01/rdf-schema#comment"The mechanism of proton pumping by P-type H(+)-ATPases is still unclear. In the plant P-type plasma membrane H(+)-ATPase AHA2, two charged residues, Arg(655) and Asp(684), are conserved in transmembrane segments M5 and M6, respectively, a region that has been shown be contribute to ion coordination in related P-type ATPases. Substitution of Arg(655) with either alanine or aspartate resulted in mutant enzymes exhibiting a significant shift in the P-type ATPase E(1)P-E(2)P conformational equilibrium. The mutant proteins accumulated in the E(1)P conformation, but were capable of conducting proton transport. This points to an important role of Arg(655) in the E(1)P-E(2)P conformational transition. The presence of a carboxylate moiety at position Asp(684) proved essential for coupling between initial proton binding and proton pumping. The finding that the carboxylate side chain of Asp(684) contributes to the proton-binding site and appears to function as an absolutely essential proton acceptor along the proton transport pathway is discussed in the context of a possible proton pumping mechanism of P-type H(+)-ATPases."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m212729200"xsd:string
http://purl.uniprot.org/citations/12626496http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m212729200"xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/author"Buch-Pedersen M.J."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/author"Buch-Pedersen M.J."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/author"Palmgren M.G."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/author"Palmgren M.G."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/pages"17845-17851"xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/pages"17845-17851"xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/title"Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/title"Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation."xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12626496http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12626496http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12626496
http://purl.uniprot.org/citations/12626496http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12626496
http://purl.uniprot.org/citations/12626496http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12626496
http://purl.uniprot.org/citations/12626496http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12626496
http://purl.uniprot.org/uniprot/P19456http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12626496
http://purl.uniprot.org/uniprot/P19456#attribution-1332D5852316AB976F7F7D5C94465314http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12626496