Linked Life Data

14993670

Source:http://linkedlifedata.com/resource/pubmed/id/14993670

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2004-3-2
pubmed:databankReference
pubmed:abstractText
The structure of the type II dehydroquinate dehydratase (DHQase) from Actinobacillus pleuropneumoniae, the third enzyme of the shikimate pathway, has been determined. Crystals diffracting to 1.7 A were obtained in space and on earth using the counter-diffusion technique. The structure was solved using molecular replacement and refined to high resolution. The overall structure of the dodecameric enzyme is described and compared with structures of DHQases from other bacteria. DHQases contain a flexible loop that presumably closes over the active site upon substrate binding. The enzyme can exist in an open or closed conformation. The present structure displays the open conformation, with a sulfate anion bound in the active site. The availability of this structure opens a route to structure-based antibiotics targetting this pathogenic bacterium.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
463-71
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae.
pubmed:affiliation
ULTR, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Pleinlaan 2, 1050 Brussels, Belgium. dominique.maes@vub.ac.be
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't