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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Suveyzdis, Yan Blessenohl, Marco Goody, Roger S. Gerwert, Klaus Kötting, Carsten Wittinghofer, Alfred |
| Description | Author Affiliation: Kötting C ( Lehrstuhl für Biophysik and Institut für Physiologische Chemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany.); |
| Abstract | The hydrolysis of nucleoside triphosphates by enzymes is used as a regulation mechanism in key biological processes. Here, the GTP hydrolysis of the protein complex of Ras with its GTPase-activating protein is monitored at atomic resolution in a noncrystalline state by time-resolved FTIR spectroscopy. At 900 ms, after the attack of water at the gamma-phosphate, there appears a H2PO4- intermediate that is shown to be hydrogen-bonded in an eclipsed conformation to the beta-phosphate of GDP. The H2PO4- intermediate is in a position where it can either reform GTP or be released from the protein in 7 s in the rate-limiting step of the GTPase reaction. We propose that such an intermediate also occurs in other GTPases and ATPases. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 38 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Protein Conformation Ras GTPase-Activating Proteins Chemistry Ras Proteins Binding Sites Enzyme Activation Guanosine Triphosphate Metabolism Hydrogen Bonding Models, Molecular Molecular Structure Phosphates Protons Spectroscopy, Fourier Transform Infrared Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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