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  The structure of the EF‐Tu · GDP · Me2+ complex

Wittinghofer, A., Goody, R. S., Rösch, P., & Kalbitzer, H. R. (1982). The structure of the EF‐Tu · GDP · Me2+ complex. European Journal of Biochemistry, 124(1), 109-115. doi:10.1111/j.1432-1033.1982.tb05912.x.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-399F-9 Version Permalink: https://hdl.handle.net/21.11116/0000-000A-3061-2
Genre: Journal Article

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EurJBiochem_124_1982_109.pdf (Any fulltext), 683KB
 
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 Creators:
Wittinghofer, Alfred1, Author           
Goody, Roger S.2, Author           
Rösch, Paul1, Author           
Kalbitzer, Hans Robert1, Author           
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1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1981-11-301982-01-252005-03-031982-05
 Publication Status: Issued
 Pages: 7
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 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1432-1033.1982.tb05912.x
URI: https://www.ncbi.nlm.nih.gov/pubmed/7200884
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 124 (1) Sequence Number: - Start / End Page: 109 - 115 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040