Publikation: Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII
Lade...
Dateien
Datum
2012
Autor:innen
Moncrieffe, Martin C.
Fernandez, Maria-Jose
Matsumura, Hiroyoshi
Gay, Nicholas J.
Luisi, Ben F.
Leadlay, Peter F.
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
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Journal of Molecular Biology. 2012, 415(1), pp. 92-101. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/j.jmb.2011.10.036
Zusammenfassung
In the biosynthesis of the clinically important antibiotic erythromycin D, the glycosyltransferase (GT) EryCIII, in concert with its partner EryCII, attaches a nucleotide-activated sugar to the macrolide scaffold with high specificity. To understand the role of EryCII, we have determined the crystal structure of the EryCIII·EryCII complex at 3.1 Å resolution. The structure reveals a heterotetramer with a distinctive, elongated quaternary organization. The EryCIII subunits form an extensive self-complementary dimer interface at the center of the complex, and the EryCII subunits lie on the periphery. EryCII binds in the vicinity of the putative macrolide binding site of EryCIII but does not make direct interactions with this site. Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690
MONCRIEFFE, Martin C., Maria-Jose FERNANDEZ, Dieter SPITELLER, Hiroyoshi MATSUMURA, Nicholas J. GAY, Ben F. LUISI, Peter F. LEADLAY, 2012. Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII. In: Journal of Molecular Biology. 2012, 415(1), pp. 92-101. ISSN 0022-2836. eISSN 1089-8638. Available under: doi: 10.1016/j.jmb.2011.10.036BibTex
@article{Moncrieffe2012-01-06Struc-20844,
year={2012},
doi={10.1016/j.jmb.2011.10.036},
title={Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII},
number={1},
volume={415},
issn={0022-2836},
journal={Journal of Molecular Biology},
pages={92--101},
author={Moncrieffe, Martin C. and Fernandez, Maria-Jose and Spiteller, Dieter and Matsumura, Hiroyoshi and Gay, Nicholas J. and Luisi, Ben F. and Leadlay, Peter F.}
}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/123456789/20844">
<dc:contributor>Spiteller, Dieter</dc:contributor>
<dc:contributor>Fernandez, Maria-Jose</dc:contributor>
<dc:contributor>Leadlay, Peter F.</dc:contributor>
<dc:creator>Gay, Nicholas J.</dc:creator>
<foaf:homepage rdf:resource="http://localhost:8080/"/>
<dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dcterms:issued>2012-01-06</dcterms:issued>
<dc:language>eng</dc:language>
<dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
<dcterms:abstract xml:lang="eng">In the biosynthesis of the clinically important antibiotic erythromycin D, the glycosyltransferase (GT) EryCIII, in concert with its partner EryCII, attaches a nucleotide-activated sugar to the macrolide scaffold with high specificity. To understand the role of EryCII, we have determined the crystal structure of the EryCIII·EryCII complex at 3.1 Å resolution. The structure reveals a heterotetramer with a distinctive, elongated quaternary organization. The EryCIII subunits form an extensive self-complementary dimer interface at the center of the complex, and the EryCII subunits lie on the periphery. EryCII binds in the vicinity of the putative macrolide binding site of EryCIII but does not make direct interactions with this site. Our biophysical and enzymatic data support a model in which EryCII stabilizes EryCIII and also functions as an allosteric activator of the GT.</dcterms:abstract>
<dc:creator>Fernandez, Maria-Jose</dc:creator>
<dc:contributor>Moncrieffe, Martin C.</dc:contributor>
<dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20844/2/Structure%20of%20the%20Glycosyltransferase%20208441.pdf"/>
<dcterms:title>Structure of the Glycosyltransferase EryCIII in Complex with its Activating P450 Homologue EryCII</dcterms:title>
<dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-19T07:43:13Z</dc:date>
<dc:contributor>Matsumura, Hiroyoshi</dc:contributor>
<dc:creator>Matsumura, Hiroyoshi</dc:creator>
<bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20844"/>
<dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-11-19T07:43:13Z</dcterms:available>
<dc:creator>Luisi, Ben F.</dc:creator>
<dc:creator>Moncrieffe, Martin C.</dc:creator>
<void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
<dcterms:bibliographicCitation>Journal of Molecular Biology ; 415 (2012), 1. - S. 92-101</dcterms:bibliographicCitation>
<dc:contributor>Gay, Nicholas J.</dc:contributor>
<dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20844/2/Structure%20of%20the%20Glycosyltransferase%20208441.pdf"/>
<dc:rights>terms-of-use</dc:rights>
<dc:creator>Leadlay, Peter F.</dc:creator>
<dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dc:creator>Spiteller, Dieter</dc:creator>
<dc:contributor>Luisi, Ben F.</dc:contributor>
</rdf:Description>
</rdf:RDF>Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
