Publikation:

Structure and assembly of the pseudopilin PulG

Lade...
Vorschaubild

Dateien

Datum

2004

Autor:innen

Köhler, Rolf
Müller, Shirley
Vignon, Guillaume
Philippsen, Ansgar
Ringler, Philippe
Pugsley, Anthony P.
Engel, Andreas

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Molecular Microbiology. 2004, 54(3), pp. 647-664. ISSN 0950-382X. eISSN 1365-2958. Available under: doi: 10.1111/j.1365-2958.2004.04307.x

Zusammenfassung

The pseudopilin PulG is one of several essential components of the type II pullulanase secretion machinery (the Pul secreton) of the Gram-negative bacterium Klebsiella oxytoca. The sequence of the N-terminal 25 amino acids of the PulG precursor is hydrophobic and very similar to the corresponding region of type IV pilins. The structure of a truncated PulG (lacking the homologous region), as determined by X-ray crystallography, was found to include part of the long N-terminal a-helix and the four internal anti-parallel b-strands that characterize type IV pilins, but PulG lacks the highly variable loop region with a disulphide bond that is found in the latter. When overproduced, PulG forms flexible pili whose structural features, as visualized by electron microscopy, are similar to those of bacterial type IV pili. The average helical repeat comprises 17 PulG subunits and four helical turns. Electron microscopy and molecular modelling show that PulG probably assembles into left-handed helical pili with the long N-terminal a-helix tightly packed in the centre of the pilus. As in the type IV pilins, the hydrophobic N-terminal part of the PulG a-helix is necessary for its assembly. Subtle sequence variations within this highly conserved segment seem to determine whether or not a type IV pilin can be assembled into pili by the Pul secreton.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690KÖHLER, Rolf, Karsten SCHÄFER, Shirley MÜLLER, Guillaume VIGNON, Kay DIEDERICHS, Ansgar PHILIPPSEN, Philippe RINGLER, Anthony P. PUGSLEY, Andreas ENGEL, Wolfram WELTE, 2004. Structure and assembly of the pseudopilin PulG. In: Molecular Microbiology. 2004, 54(3), pp. 647-664. ISSN 0950-382X. eISSN 1365-2958. Available under: doi: 10.1111/j.1365-2958.2004.04307.x
BibTex
@article{Kohler2004Struc-8617,
  year={2004},
  doi={10.1111/j.1365-2958.2004.04307.x},
  title={Structure and assembly of the pseudopilin PulG},
  number={3},
  volume={54},
  issn={0950-382X},
  journal={Molecular Microbiology},
  pages={647--664},
  author={Köhler, Rolf and Schäfer, Karsten and Müller, Shirley and Vignon, Guillaume and Diederichs, Kay and Philippsen, Ansgar and Ringler, Philippe and Pugsley, Anthony P. and Engel, Andreas and Welte, Wolfram}
}
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/123456789/8617">
    <dc:contributor>Vignon, Guillaume</dc:contributor>
    <dc:creator>Ringler, Philippe</dc:creator>
    <dc:contributor>Pugsley, Anthony P.</dc:contributor>
    <dc:language>eng</dc:language>
    <dcterms:title>Structure and assembly of the pseudopilin PulG</dcterms:title>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8617/1/Structure_and_assembly_of_the_pseudopilin_PulG.pdf"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dc:creator>Philippsen, Ansgar</dc:creator>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Engel, Andreas</dc:contributor>
    <dcterms:issued>2004</dcterms:issued>
    <dc:creator>Müller, Shirley</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:08Z</dcterms:available>
    <dc:creator>Vignon, Guillaume</dc:creator>
    <dc:creator>Köhler, Rolf</dc:creator>
    <dc:contributor>Welte, Wolfram</dc:contributor>
    <dc:format>application/pdf</dc:format>
    <dc:creator>Diederichs, Kay</dc:creator>
    <dc:creator>Welte, Wolfram</dc:creator>
    <dc:contributor>Schäfer, Karsten</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:08Z</dc:date>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8617/1/Structure_and_assembly_of_the_pseudopilin_PulG.pdf"/>
    <dc:creator>Schäfer, Karsten</dc:creator>
    <dc:creator>Pugsley, Anthony P.</dc:creator>
    <dc:contributor>Köhler, Rolf</dc:contributor>
    <dc:creator>Engel, Andreas</dc:creator>
    <dc:contributor>Müller, Shirley</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Philippsen, Ansgar</dc:contributor>
    <dcterms:abstract xml:lang="deu">The pseudopilin PulG is one of several essential components of the type II pullulanase secretion machinery (the Pul secreton) of the Gram-negative bacterium Klebsiella oxytoca. The sequence of the N-terminal 25 amino acids of the PulG precursor is hydrophobic and very similar to the corresponding region of type IV pilins. The structure of a truncated PulG (lacking the homologous region), as determined by X-ray crystallography, was found to include part of the long N-terminal a-helix and the four internal anti-parallel b-strands that characterize type IV pilins, but PulG lacks the highly variable loop region with a disulphide bond that is found in the latter. When overproduced, PulG forms flexible pili whose structural features, as visualized by electron microscopy, are similar to those of bacterial type IV pili. The average helical repeat comprises 17 PulG subunits and four helical turns. Electron microscopy and molecular modelling show that PulG probably assembles into left-handed helical pili with the long N-terminal a-helix tightly packed in the centre of the pilus. As in the type IV pilins, the hydrophobic N-terminal part of the PulG a-helix is necessary for its assembly. Subtle sequence variations within this highly conserved segment seem to determine whether or not a type IV pilin can be assembled into pili by the Pul secreton.</dcterms:abstract>
    <dc:contributor>Ringler, Philippe</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8617"/>
    <dcterms:bibliographicCitation>First publ. in: Molecular Microbiology 54 (2004), 3, pp. 647-664</dcterms:bibliographicCitation>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Diese Publikation teilen