Linked Life Data

12777763

Source:http://linkedlifedata.com/resource/pubmed/id/12777763

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 6
pubmed:dateCreated
2003-6-2
pubmed:databankReference
pubmed:abstractText
The Escherichia coli adhesin F17-G is a carbohydrate-binding protein that allows the bacterium to attach to the intestinal epithelium of young ruminants. The structure of the 17 kDa lectin domain of F17-G was determined using the anomalous dispersion signal of a selenium-containing analogue of the monosaccharide ligand N-acetyl-d-glucosamine in which the anomeric oxygen was replaced by an Se atom. A three-wavelength MAD data set yielded good experimental phases to 2.6 A resolution. The structure was refined to 1.75 A resolution and was used to solve the structures of the ligand-free protein and the F17-G-N-acetyl-d-glucosamine complex. This selenium-carbohydrate phasing method could be of general use for determining the structures of carbohydrate-binding proteins.
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
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1012-5
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin.
pubmed:affiliation
Department of Ultrastructure, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Pleinlaan 2, 1050 Brussels, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't