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Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB

Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB

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KRUG, Michael, Sung-Jae LEE, Kay DIEDERICHS, Winfried BOOS, Wolfram WELTE, 2006. Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB. In: Journal of Biological Chemistry. 281(16), pp. 10976-10982. ISSN 0021-9258. eISSN 1083-351X

@article{Krug2006Cryst-7898, title={Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB}, year={2006}, doi={10.1074/jbc.M512809200}, number={16}, volume={281}, issn={0021-9258}, journal={Journal of Biological Chemistry}, pages={10976--10982}, author={Krug, Michael and Lee, Sung-Jae and Diederichs, Kay and Boos, Winfried and Welte, Wolfram} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7898"> <dc:format>application/pdf</dc:format> <dcterms:abstract xml:lang="eng">TrmB is an alpha-glucoside-sensing transcriptional regulator controlling two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus furiosus. The crystal structure of an N-terminal truncated derivative of TrmB was solved at 1.5A resolution. This protein has lost its DNA binding domain but has retained its sugar recognition site. The structure represents a novel sugar-binding fold. TrmB bound maltose, glucose, sucrose, and maltotriose, exhibiting Kd values of 6.8, 25, 34, and 160 μM, respectively. TrmB behaved as a monomer in dilute buffer solution in contrast to the full-length protein, which is a dimer. Co-crystallization with bound maltose identified a binding site involving seven amino acid residues: Ser229, Asn305, Gly320, Met321, Val324, Ile325, and Glu326. Six of these residues interact with the nonreducing glucosyl residue of maltose. The nonreducing glucosyl residue is shared by all substrates bound to TrmB, suggesting it as a common recognition motif.</dcterms:abstract> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:22Z</dc:date> <dc:contributor>Diederichs, Kay</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:22Z</dcterms:available> <dc:creator>Diederichs, Kay</dc:creator> <dc:contributor>Krug, Michael</dc:contributor> <dc:creator>Boos, Winfried</dc:creator> <dc:contributor>Boos, Winfried</dc:contributor> <dc:creator>Welte, Wolfram</dc:creator> <dcterms:issued>2006</dcterms:issued> <dc:contributor>Lee, Sung-Jae</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 281 (2006), 16, pp. 10976-10982</dcterms:bibliographicCitation> <dc:creator>Lee, Sung-Jae</dc:creator> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7898"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:creator>Krug, Michael</dc:creator> <dc:contributor>Welte, Wolfram</dc:contributor> <dcterms:title>Crystal Structure of the Sugar Binding Domain of the Archaeal Transcritional Regulator TrmB</dcterms:title> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

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