Linked Life Data

12037321

Source:http://linkedlifedata.com/resource/pubmed/id/12037321

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6 Pt 2
pubmed:dateCreated
2002-5-30
pubmed:abstractText
Enoyl-acyl carrier protein reductase (ENR) catalyzes the NADH-dependent stereospecific reduction of alpha,beta-unsaturated fatty acids bound to the acyl-carrier protein. ENR from Helicobacter pylori has been overexpressed in Escherichia coli and has been crystallized in the presence of its cofactor NADH and the inhibitor triclosan (or its analogue diclosan) at 296 K using polyethylene glycol (PEG) 400 as a precipitant. For the triclosan (or diclosan) complex, diffraction data to 2.5 (or 2.3) A resolution have been collected using synchrotron X-rays. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 73.35, b = 94.91, c = 75.38 A, beta = 106.21 degrees for the triclosan complex (or a = 73.25, b = 95.07, c = 75.02 A, beta = 106.53 degrees for the diclosan complex). The asymmetric unit contains one homotetramer, with a corresponding V(M) of 2.10 A(3) Da(-1) and a solvent content of 41% by volume.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1071-3
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Crystallization and preliminary X-ray crystallographic analysis of enoyl-acyl carrier protein reductase from Helicobacter pylori.
pubmed:affiliation
Laboratory of Structural Proteomics, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
pubmed:publicationType
Journal Article