Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose

Hars, Ulrike; Horlacher, Reinhold; Boos, Winfried; Welte, Wolfram; Diederichs, Kay

Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose

Dateien

33_trer.pdfGröße: 11.15 MBDownloads: 432

Datum

1998

Autor:innen

Hars, Ulrike

Horlacher, Reinhold

Boos, Winfried

Welte, Wolfram

Diederichs, Kay

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Protein Science. 1998, 7(12), pp. 2511-2521. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1002/pro.5560071204

Zusammenfassung

The crystal structure of the Escherichia coli trehalose repressor (TreR) in a complex with its inducer trehalose-6-phosphate was determined by the method of multiple isomorphous replacement (MIR) at 2.5 Å resolution, followed by the structure determination of TreR in a complex with its noninducer trehalose at 3.1 Å resolution. The model consists of residues 61 to 315 comprising the effector binding domain, which forms a dimer as in other members of the LacI family. This domain is composed of two similar subdomains each consisting of a central β-sheet sandwiched between α-helices. The effector binding pocket is at the interface of these subdomains. In spite of different physiological functions, the crystal structures of the two complexes of TreR turned out to be virtually identical to each other with the conformation being similar to those of the effector binding domains of the LacI and PurR in complex with their effector molecules. According to the crystal structure, the noninducer trehalose binds to a similar site as the trehalose portion of trehalose-6-phosphate. The binding affinity for the former is lower than for the latter. The noninducer trehalose thus binds competitively to the repressor. Unlike the phosphorylated inducer molecule, it is incapable of blocking the binding of the repressor headpiece to its operator DNA. The ratio of the concentrations of trehalose-6-phosphate and trehalose thus is used to switch between the two alternative metabolic uses of trehalose as an osmoprotectant and as a carbon source.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

LacI family, phosphate binding, protein structure, trehalose repressor

Zitieren

ISO 690

HARS, Ulrike, Reinhold HORLACHER, Winfried BOOS, Wolfram WELTE, Kay DIEDERICHS, 1998. Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose. In: Protein Science. 1998, 7(12), pp. 2511-2521. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1002/pro.5560071204

BibTex

@article{Hars1998Cryst-6728,
  year={1998},
  doi={10.1002/pro.5560071204},
  title={Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose},
  number={12},
  volume={7},
  issn={0961-8368},
  journal={Protein Science},
  pages={2511--2521},
  author={Hars, Ulrike and Horlacher, Reinhold 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/123456789/6728">
    <dc:creator>Hars, Ulrike</dc:creator>
    <dc:contributor>Boos, Winfried</dc:contributor>
    <dc:contributor>Horlacher, Reinhold</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:45Z</dc:date>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6728/1/33_trer.pdf"/>
    <dcterms:title>Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose</dcterms:title>
    <dc:contributor>Welte, Wolfram</dc:contributor>
    <dcterms:issued>1998</dcterms:issued>
    <dc:language>eng</dc:language>
    <dc:creator>Welte, Wolfram</dc:creator>
    <dc:contributor>Hars, Ulrike</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:bibliographicCitation>First publ. in: Protein Science 7 (1998), pp. 2511-2521</dcterms:bibliographicCitation>
    <dcterms:abstract xml:lang="eng">The crystal structure of the Escherichia coli trehalose repressor (TreR) in a complex with its inducer trehalose-6-phosphate was determined by the method of multiple isomorphous replacement (MIR) at 2.5 Å resolution, followed by the structure determination of TreR in a complex with its noninducer trehalose at 3.1 Å resolution. The model consists of residues 61 to 315 comprising the effector binding domain, which forms a dimer as in other members of the LacI family. This domain is composed of two similar subdomains each consisting of a central β-sheet sandwiched between α-helices. The effector binding pocket is at the interface of these subdomains. In spite of different physiological functions, the crystal structures of the two complexes of TreR turned out to be virtually identical to each other with the conformation being similar to those of the effector binding domains of the LacI and PurR in complex with their effector molecules. According to the crystal structure, the noninducer trehalose binds to a similar site as the trehalose portion of trehalose-6-phosphate. The binding affinity for the former is lower than for the latter. The noninducer trehalose thus binds competitively to the repressor. Unlike the phosphorylated inducer molecule, it is incapable of blocking the binding of the repressor headpiece to its operator DNA. The ratio of the concentrations of trehalose-6-phosphate and trehalose thus is used to switch between the two alternative metabolic uses of trehalose as an osmoprotectant and as a carbon source.</dcterms:abstract>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/6728/1/33_trer.pdf"/>
    <dc:creator>Boos, Winfried</dc:creator>
    <dc:format>application/pdf</dc:format>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dc:creator>Horlacher, Reinhold</dc:creator>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6728"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Diederichs, Kay</dc:creator>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:28:45Z</dcterms:available>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Nein