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  • Title: A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein.
    Author: Kötting C, Blessenohl M, Suveyzdis Y, Goody RS, Wittinghofer A, Gerwert K.
    Journal: Proc Natl Acad Sci U S A; 2006 Sep 19; 103(38):13911-6. PubMed ID: 16968776.
    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.
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