Molecular Dynamics Simulation Studies of dTTP Binding and Catalysis Mediated by YhdE Dimerization.
YhdE is a Maf-like (multicopy associated filamentation) protein that primarily acts as dTTPase to hydrolyze dTTP into dTMP and two phosphate molecules in cell metabolism pathway. Two crystal structures of YhdE have been previously determined, representing the open and closed active site conformation...
Main Authors: | Nan Wang, Jiahong Jiang, Xichen Li, Hongwei Tan, Jimin Zheng, Guangju Chen, Zongchao Jia |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2015-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC4529217?pdf=render |
Similar Items
-
A new method to investigate the catalytic mechanism of YhdE pyrophosphatase by using a pyrophosphate fluorescence probe
by: Qingya Shen, et al.
Published: (2017-08-01) -
Insights into the cellular function of YhdE, a nucleotide pyrophosphatase from Escherichia coli.
by: Jin Jin, et al.
Published: (2015-01-01) -
Unique kinase catalytic mechanism of AceK with a single magnesium ion.
by: Quanjie Li, et al.
Published: (2013-01-01) -
The mRNA-binding Protein TTP/ZFP36 in Hepatocarcinogenesis and Hepatocellular Carcinoma
by: Tarek Kröhler, et al.
Published: (2019-11-01) -
The ARE-binding protein Tristetraprolin (TTP) is a novel target and mediator of calcineurin tumor suppressing function in the skin.
by: Xunwei Wu, et al.
Published: (2018-05-01)