TY  -  
T1  - Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation 
SN  -  /  
UR  - http://hdl.handle.net/10138/190456 
T3  -  
A1  - Shah, Nita R.; Wilkinson, Craig; Harborne, Steven P. D.; Turku, Ainoleena; Li, Kun-Mou; Sun, Yuh-Ju; Harris, Sarah; Goldman, Adrian 
A2  -  
PB  -  
Y1  - 2017 
LA  - eng 
AB  - Membrane-integral pyrophosphatases (mPPases) couple the hydrolysis of pyrophosphate (PPi) to the pumping of Na+, H+, or both these ions across a membrane. Recently solved structures of the Na+-pumping Thermotoga maritima mPPase (TmPPase) and H+-pumping Vigna radiata mPPase revealed the basis of ion selectivity between these enzymes and provided evidence for the mechanisms of substrate hydrolysis and ion-pumping. Our atomistic molecular dynamics (MD) simulations of TmPPase demonstrate that loop 5... 
VO  -  
IS  -  
SP  -  
OP  -  
KW  - H+-PYROPHOSPHATASE; PUMPING PYROPHOSPHATASE; INORGANIC PYROPHOSPHATE; MOLECULAR-DYNAMICS; FORCE-FIELD; ACIDOCALCISOMES; NA+; OVEREXPRESSION; CONSERVATION; STRESS; 116 Chemical sciences; 317 Pharmacy 
N1  -   
PP  -  
ER  -