Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The thermophilic eubacterium Thermus thermophilus belongs to one of the oldest branches of evolution and has a multilayered cell envelope that differs from that of modern Gram-negative bacteria. Its outer membrane contains integral outer membrane proteins (OMPs), of which only a few are characterized. TtoA, a new p-barrel OMP, was identified by searching the genome sequence of strain HB27 for the presence of a C-terminal signature sequence. The structure of TtoA was determined to a resolution of 2.8 Å, representing the first crystal structure of an OMP from a thermophilic bacterium. TtoA consists of an eight-stranded p-barrel with a large extracellular part to which a divalent cation is bound. A five-stranded extracellular β-sheet protrudes out of the membrane-embedded transmembrane barrel and is stabilized by a disulfide bridge. The edge of this β-sheet forms crystal contacts that could mimic interactions with other proteins. In modem Gram-negative bacteria, the C-terminal signature sequence of OMPs is required for binding to an Omp85 family protein as a prerequisite for its assembly. We present hints that a similar assembly pathway exists in T. thermophilus by an in vitro binding assay, where unfolded TtoA binds to the Thermus Omp85 family protein TtOmp85, while a mutant without the signature sequence does not.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
BROSIG, Alexander, Jutta NESPER, Winfried BOOS, Wolfram WELTE, Kay DIEDERICHS, 2009. Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27. In: Journal of Molecular Biology. 2009, 385(5), pp. 1445-1455. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/j.jmb.2008.12.003BibTex
@article{Brosig2009-02-06Cryst-1125, year={2009}, doi={10.1016/j.jmb.2008.12.003}, title={Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27}, number={5}, volume={385}, issn={0022-2836}, journal={Journal of Molecular Biology}, pages={1445--1455}, author={Brosig, Alexander and Nesper, Jutta and Boos, Winfried and Welte, Wolfram and Diederichs, Kay} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/1125"> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:rights>terms-of-use</dc:rights> <dc:contributor>Boos, Winfried</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:06:19Z</dcterms:available> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/1125"/> <dc:contributor>Welte, Wolfram</dc:contributor> <dc:contributor>Brosig, Alexander</dc:contributor> <dc:creator>Boos, Winfried</dc:creator> <dc:creator>Nesper, Jutta</dc:creator> <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/1125/1/Brosig_etal_Crystal%20Structure.pdf"/> <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/1125/1/Brosig_etal_Crystal%20Structure.pdf"/> <dc:creator>Diederichs, Kay</dc:creator> <dc:creator>Brosig, Alexander</dc:creator> <dc:language>eng</dc:language> <dcterms:issued>2009-02-06</dcterms:issued> <dc:contributor>Nesper, Jutta</dc:contributor> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:contributor>Diederichs, Kay</dc:contributor> <dcterms:bibliographicCitation>Publ. in: Journal of molecular biology 385 (2009), 5, pp. 1445-1455</dcterms:bibliographicCitation> <dcterms:title>Crystal Structure of a Major Outer Membrane Protein from Thermus thermophilus HB27</dcterms:title> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-23T09:06:19Z</dc:date> <dcterms:abstract xml:lang="eng">The thermophilic eubacterium Thermus thermophilus belongs to one of the oldest branches of evolution and has a multilayered cell envelope that differs from that of modern Gram-negative bacteria. Its outer membrane contains integral outer membrane proteins (OMPs), of which only a few are characterized. TtoA, a new p-barrel OMP, was identified by searching the genome sequence of strain HB27 for the presence of a C-terminal signature sequence. The structure of TtoA was determined to a resolution of 2.8 Å, representing the first crystal structure of an OMP from a thermophilic bacterium. TtoA consists of an eight-stranded p-barrel with a large extracellular part to which a divalent cation is bound. A five-stranded extracellular β-sheet protrudes out of the membrane-embedded transmembrane barrel and is stabilized by a disulfide bridge. The edge of this β-sheet forms crystal contacts that could mimic interactions with other proteins. In modem Gram-negative bacteria, the C-terminal signature sequence of OMPs is required for binding to an Omp85 family protein as a prerequisite for its assembly. We present hints that a similar assembly pathway exists in T. thermophilus by an in vitro binding assay, where unfolded TtoA binds to the Thermus Omp85 family protein TtOmp85, while a mutant without the signature sequence does not.</dcterms:abstract> <dc:creator>Welte, Wolfram</dc:creator> </rdf:Description> </rdf:RDF>