Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor

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BLANCK, Andreas, Elisa MAY, Ernst S. SCHEGK, Dieter OESTERHELT, Friedrich LOTTSPEICH, 1989. Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor. In: The EMBO Journal. 8(13), pp. 3963-3971. ISSN 0261-4189. eISSN 1460-2075

@article{Blanck1989Prima-22066, title={Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor}, year={1989}, number={13}, volume={8}, issn={0261-4189}, journal={The EMBO Journal}, pages={3963--3971}, author={Blanck, Andreas and May, Elisa and Schegk, Ernst S. and Oesterhelt, Dieter and Lottspeich, Friedrich} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:date rdf:datatype="">2013-03-20T11:13:55Z</dc:date> <dc:contributor>May, Elisa</dc:contributor> <dc:creator>Oesterhelt, Dieter</dc:creator> <bibo:uri rdf:resource=""/> <dc:creator>May, Elisa</dc:creator> <dc:contributor>Lottspeich, Friedrich</dc:contributor> <dc:language>eng</dc:language> <dcterms:rights rdf:resource=""/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Schegk, Ernst S.</dc:creator> <dc:rights>terms-of-use</dc:rights> <dc:creator>Lottspeich, Friedrich</dc:creator> <dspace:hasBitstream rdf:resource=""/> <dc:contributor>Oesterhelt, Dieter</dc:contributor> <dc:contributor>Schegk, Ernst S.</dc:contributor> <dcterms:bibliographicCitation>The EMBO Journal ; 8 (1989), 13. - S. 3963–3971</dcterms:bibliographicCitation> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:isPartOf rdf:resource=""/> <dc:contributor>Blanck, Andreas</dc:contributor> <dcterms:abstract xml:lang="eng">The gene coding for sensory rhodopsin I (SR-I) has been identified in a restriction fragment of genomic DNA from the Halobacterium halobium strain L33. Of the 1014 nucleotides whose sequence was determined, 720 belong to the structural gene of SR-I. In the 5' non-coding region two putative promoter elements and a ribosomal binding site have been identified. The 3' flanking region bears a potential terminator structure. The SR-I protein moiety carries no signal peptide and is not processed at its N terminus. The C terminus, however, lacks the last aspartic acid residue encoded by the gene. Analysis of the primary structure of SR-I reveals no consistent homology with the eukaryotic photoreceptor rhodopsin, but 14% homology with the halobacterial ion pumps, bacteriorhodopsin (BR) and halorhodopsin (HR). Residues conserved in all three proteins are discussed with respect to their contribution to secondary structure, retinal binding and ion translocation. The aspartic acid residue which mediates in BR the reprotonation of the Schiff base (D96) is replaced in SR-I by a tyrosine (Y87). This amino acid replacement is proposed to be of crucial importance in the evolution of the slow-cycling photosensing pigment SR-I.</dcterms:abstract> <dc:creator>Blanck, Andreas</dc:creator> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:title>Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor</dcterms:title> <dcterms:hasPart rdf:resource=""/> <dcterms:issued>1989</dcterms:issued> <dcterms:available rdf:datatype="">2013-03-20T11:13:55Z</dcterms:available> </rdf:Description> </rdf:RDF>

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