scholarly journals Analysis of Gating Process Associated with Water Permeation of the E-coli Mechanosensitive Channel MscL Using Molecular Dynamics Simulations

2009 ◽  
Vol 96 (3) ◽  
pp. 254a
Author(s):  
Yasuyuki Sawada ◽  
Masaki Murase ◽  
Masahiro Sokabe
2017 ◽  
Vol 112 (3) ◽  
pp. 501a
Author(s):  
Gladys Diaz Vazquez ◽  
Samson Condon ◽  
Qiang Cui ◽  
Alessandro Senes

2013 ◽  
Vol 104 (2) ◽  
pp. 586a ◽  
Author(s):  
Emilia L. Wu ◽  
Olof Engstrom ◽  
Sunhwan Jo ◽  
Dani Stuhlsatz ◽  
Goran Wildmalm ◽  
...  

F1000Research ◽  
2014 ◽  
Vol 3 ◽  
pp. 67 ◽  
Author(s):  
Kate A. Stafford ◽  
Arthur G. Palmer III

Ribonuclease H1 (RNase H) enzymes are well-conserved endonucleases that are present in all domains of life and are particularly important in the life cycle of retroviruses as domains within reverse transcriptase. Despite extensive study, especially of the E. coli homolog, the interaction of the highly negatively charged active site with catalytically required magnesium ions remains poorly understood. In this work, we describe molecular dynamics simulations of the E. coli homolog in complex with magnesium ions, as well as simulations of other homologs in their apo states. Collectively, these results suggest that the active site is highly rigid in the apo state of all homologs studied and is conformationally preorganized to favor the binding of a magnesium ion. Notably, representatives of bacterial, eukaryotic, and retroviral RNases H all exhibit similar active-site rigidity, suggesting that this dynamic feature is only subtly modulated by amino acid sequence and is primarily imposed by the distinctive RNase H protein fold.


Sign in / Sign up

Export Citation Format

Share Document