Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19 F NMR, and DFT Approaches-Reference-Cited by-同舟云学术

Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19 F NMR, and DFT Approaches

Published:2017-05-24 Issue:33 Volume:129 Page:9864-9867
ISSN:0044-8249
Container-title:Angewandte Chemie
language:en
Short-container-title:Angew. Chem.

Author:

Jin Yi¹²^ORCID,Molt Robert W.²³⁴,Pellegrini Erika⁵,Cliff Matthew J.⁶,Bowler Matthew W.⁵⁷,Richards Nigel G. J.²,Blackburn G. Michael¹,Waltho Jonathan P.¹⁶

Affiliation:

1. Department of Molecular Biology and BiotechnologyKrebs InstituteUniversity of Sheffield Sheffield S10 2TN UK

2. School of ChemistryCardiff University Cardiff CF10 3AT UK

3. Department of Biochemistry and Molecular BiologyIndiana University School of Medicine Indianapolis IN 46202 USA

4. ENSCO, Inc. Melbourne FL 32940 USA

5. Structural Biology GroupESRF-The European Synchrotron, CS40220 38043 Grenoble, Cedex 9 France

6. Manchester Institute of Biotechnology Manchester M1 7DN UK

7. European Molecular Biology Laboratory, Grenoble Outstation CS90181 38042 Grenoble, Cedex 9 France

Funder

Biotechnology and Biological Sciences Research Council

Publisher

Wiley

Subject

General Medicine

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/ange.201703074

Reference34 articles.

2. A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site

3. Anionic Charge Is Prioritized over Geometry in Aluminum and Magnesium Fluoride Transition State Analogs of Phosphoryl Transfer Enzymes

4. MgF3− and α-Galactose 1-Phosphate in the Active Site of β-Phosphoglucomutase Form a Transition State Analogue of Phosphoryl Transfer

5. Transition State Analogue Structures of Human Phosphoglycerate Kinase Establish the Importance of Charge Balance in Catalysis

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