Induced-fit movements in adenylate kinases

Schulz, Georg E.; Müller, Christoph W.; Diederichs, Kay

Induced-fit movements in adenylate kinases

Dateien

schulz_208664.pdfGröße: 431.92 KBDownloads: 578

Datum

1990

Autor:innen

Schulz, Georg E.

Müller, Christoph W.

Diederichs, Kay

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Journal of Molecular Biology. 1990, 213(4), pp. 627-630. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/S0022-2836(05)80250-5

Zusammenfassung

The high-resolution crystal structures of three homologous adenylate kinases with zero, one and both (= 2-substrate mimicking inhibitor) bound substrates have been compared. The comparisons are meaningful, because all structures occur in two or three different crystal contact environments indicating that they represent intrinsically stable conformations in solution. Molecular superimpositions revealed that two domains comprising 30 and 38 residues undergo large movements on substrate binding, which can be approximated by rigid-body rotations over 39° and 92°, respectively. Moreover, these movements can be subdivided into two steps: first, a change on binding substrate AMP, which involves only the 30 residue domain (Cα shifts up to 8·2 Å), and second, a change on additional binding of substrate ATP, which again involves the 30 residue domain (Cα shifts up to 7·6 Å) but also the 38 residue domain (Cα shifts up to 32·3 Å). Taken together, these observations yield a three-picture "moving film" of the induced-fit.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

SCHULZ, Georg E., Christoph W. MÜLLER, Kay DIEDERICHS, 1990. Induced-fit movements in adenylate kinases. In: Journal of Molecular Biology. 1990, 213(4), pp. 627-630. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/S0022-2836(05)80250-5

BibTex

@article{Schulz1990Induc-20866,
  year={1990},
  doi={10.1016/S0022-2836(05)80250-5},
  title={Induced-fit movements in adenylate kinases},
  number={4},
  volume={213},
  issn={0022-2836},
  journal={Journal of Molecular Biology},
  pages={627--630},
  author={Schulz, Georg E. and Müller, Christoph W. 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/123456789/20866">
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:title>Induced-fit movements in adenylate kinases</dcterms:title>
    <dc:contributor>Schulz, Georg E.</dc:contributor>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20866/1/schulz_208664.pdf"/>
    <dc:contributor>Müller, Christoph W.</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <dc:creator>Diederichs, Kay</dc:creator>
    <dc:creator>Schulz, Georg E.</dc:creator>
    <dcterms:issued>1990</dcterms:issued>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20866/1/schulz_208664.pdf"/>
    <dc:language>eng</dc:language>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dcterms:bibliographicCitation>Journal of Molecular Biology ; 213 (1990), 4. - S. 627-630</dcterms:bibliographicCitation>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-16T06:50:56Z</dc:date>
    <dc:creator>Müller, Christoph W.</dc:creator>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:abstract xml:lang="eng">The high-resolution crystal structures of three homologous adenylate kinases with zero, one and both (= 2-substrate mimicking inhibitor) bound substrates have been compared. The comparisons are meaningful, because all structures occur in two or three different crystal contact environments indicating that they represent intrinsically stable conformations in solution. Molecular superimpositions revealed that two domains comprising 30 and 38 residues undergo large movements on substrate binding, which can be approximated by rigid-body rotations over 39° and 92°, respectively. Moreover, these movements can be subdivided into two steps: first, a change on binding substrate AMP, which involves only the 30 residue domain (Cα shifts up to 8·2 Å), and second, a change on additional binding of substrate ATP, which again involves the 30 residue domain (Cα shifts up to 7·6 Å) but also the 38 residue domain (Cα shifts up to 32·3 Å). Taken together, these observations yield a three-picture "moving film" of the induced-fit.</dcterms:abstract>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-16T06:50:56Z</dcterms:available>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20866"/>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Nein