Linked Life Data

7200884

Source:http://linkedlifedata.com/resource/pubmed/id/7200884

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1982-8-7
pubmed:abstractText
The structure of the MgGDP complex at the active site of elongation factor (EF-Tu) has been investigated by using phosphorothioate analogs of GDP in the absence and presence of various metal ions, electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) measurements. The high stereoselectivity of EF-Tu for the diastereomers of guanosine 5'-O-(1-thiodiphosphate) (GDP[alpha S]) is independent of the nature of the metal ion and is caused by the interaction of the protein with the alpha-phosphate of GDP. By using GDP analogs where the oxygens at either the alpha-phosphate or the beta-phosphate have been selectively labelled with 17O and measuring their effect on the EPR spectrum of EF-Tu-bound manganese we are able to show that only the beta-phosphate of GDP is coordinated to the metal ion in the EF-Tu . Me2+ . GDP complex. 31P-NMR studies on GDP and guanosine 5'-O-(2-thiodiphosphate) (GDP[beta S]) bound to EF-Tu indicate that in the EF-Tu . Me2+ . GDP complex Mg2+ interacts more strongly with the beta-phosphate than with the alpha-phosphate. Together with binding studies using GDP[beta S] our NMR results also indicate that the protein is complexed to the beta-phosphorous of GDP via two oxygens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
109-15
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
The structure of the EF-Tu . GDP . Me2+ complex.
pubmed:publicationType
Journal Article