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Siderophore-Mediated Iron Transport : Crystal Structure of FhuA with Bound Lipopolysaccharide

Siderophore-Mediated Iron Transport : Crystal Structure of FhuA with Bound Lipopolysaccharide

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FERGUSON, Andrew D., Eckhard HOFMANN, James W. COULTON, Kay DIEDERICHS, Wolfram WELTE, 1998. Siderophore-Mediated Iron Transport : Crystal Structure of FhuA with Bound Lipopolysaccharide. In: Science. 282(5397), pp. 2215-2220

@article{Ferguson1998Sider-8631, title={Siderophore-Mediated Iron Transport : Crystal Structure of FhuA with Bound Lipopolysaccharide}, year={1998}, doi={10.1126/science.282.5397.2215}, number={5397}, volume={282}, journal={Science}, pages={2215--2220}, author={Ferguson, Andrew D. and Hofmann, Eckhard and Coulton, James W. and Diederichs, Kay 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/123456789/8631"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:15Z</dc:date> <dc:creator>Welte, Wolfram</dc:creator> <dc:contributor>Welte, Wolfram</dc:contributor> <dc:creator>Hofmann, Eckhard</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:15Z</dcterms:available> <dcterms:bibliographicCitation>First publ. in: Science 282 (1998), pp. 2215-2220</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a family of integral outer membrane proteins, which, together with the energytransducing protein TonB, mediate the active transport of ferric siderophores across the outer membrane of Gram-negative bacteria. The three-dimensional structure of FhuA is presented here in two conformations: with and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms, respectively. FhuA is a β barrel composed of 22 antiparallel β strands. In contrast to the typical trimeric arrangement found in porins, FhuA is monomeric. Located within the β barrel is a structurally distinct domain, the "cork," which mainly consists of a four-stranded β sheet and four short α helices. A single lipopolysaccharide molecule is noncovalently associated with the membrane-embedded region of the protein. Upon binding of ferrichrome-iron, conformational changes are transduced to the periplasmic pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence homologies and mutagenesis data are used to propose a structural mechanism for TonB-dependent siderophore-mediated transport across the outer membrane.</dcterms:abstract> <dc:creator>Diederichs, Kay</dc:creator> <dc:contributor>Coulton, James W.</dc:contributor> <dc:language>eng</dc:language> <dcterms:issued>1998</dcterms:issued> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:format>application/pdf</dc:format> <dcterms:title>Siderophore-Mediated Iron Transport : Crystal Structure of FhuA with Bound Lipopolysaccharide</dcterms:title> <dc:contributor>Diederichs, Kay</dc:contributor> <dc:contributor>Hofmann, Eckhard</dc:contributor> <dc:creator>Ferguson, Andrew D.</dc:creator> <dc:contributor>Ferguson, Andrew D.</dc:contributor> <dc:creator>Coulton, James W.</dc:creator> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8631"/> </rdf:Description> </rdf:RDF>

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