Electrostatic interactions determine entrance/release order of substrates in the catalytic cycle of adenylate kinase-Reference-Cited by-同舟云学术

Electrostatic interactions determine entrance/release order of substrates in the catalytic cycle of adenylate kinase

Published:2019-01-17 Issue:4 Volume:87 Page:337-347
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Ye Chun¹²,Ding Chengtao²,Ma Rongsheng²,Wang Junfeng¹,Zhang Zhiyong²^ORCID

Affiliation:

1. High Magnetic Field Laboratory; Chinese Academy of Sciences; Hefei Anhui China

2. Hefei National Laboratory for Physical Science at Microscale and School of Life Sciences; University of Science and Technology of China; Hefei Anhui China

Funder

the National Natural Science Foundation of China

The Strategic Priority Research Program (Pilot study): "Biological basis of aging and therapeutic strategies" of the Chinese Academy of Sciences

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.25655/fullpdf

Reference54 articles.

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2. Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 Å resolution: a model for a catalytic transition state;Müller;J Mol Biol,1992

3. Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop;Müller;Proteins,1993

4. The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP;Berry;Proteins,1994

5. High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer;Abele;Protein Sci,1995

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