A GAP‐GTPase‐GDP‐P i Intermediate Crystal Structure Analyzed by DFT Shows GTP Hydrolysis Involves Serial Proton Transfers-Reference-Cited by-同舟云学术

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A GAP‐GTPase‐GDP‐P i Intermediate Crystal Structure Analyzed by DFT Shows GTP Hydrolysis Involves Serial Proton Transfers

Published:2019-05-27 Issue:36 Volume:25 Page:8484-8488
ISSN:0947-6539
Container-title:Chemistry – A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

Molt Robert W.¹²,Pellegrini Erika³,Jin Yi⁴^ORCID

Affiliation:

1. Department of Biochemistry & Molecular BiologyIndiana University School of Medicine Indianapolis Indiana 46202 USA

2. ENSCO, Inc. 4849 North Wickham Road Melbourne Florida 32940 USA

3. 9 European Molecular Biology Laboratory 71 Avenue des Martyrs, CS 90181 38042 Grenoble, Cedex 9 France

4. Cardiff Catalysis InstituteSchool of ChemistryCardiff University Cardiff CF10 3AT UK

Funder

Wellcome Trust

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.201901627

Reference42 articles.

1.

2. The Mechanism of Ras GTPase Activation by Neurofibromin

3. Kinetics of Inorganic Phosphate Release during the Interaction of p21ras with the GTPase-Activating Proteins, p120-GAP and Neurofibromin

4. The GAP arginine finger movement into the catalytic site of Ras increases the activation entropy

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