Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 27, Issue -, Pages 38-47Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.03.007
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Funding
- Ministry of Science and Technology, Taiwan [NSC 101-2311-B-007-009-MY3]
- Academia Sinica, Taiwan [AS-103-TP-B11]
- National Graduate School in Informational and Structural Biology (ISB)
- European Drug Initiative on Channels and Transporters (EDICT) project
- Sigrid Juselius Foundation
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Membrane-bound pyrophosphatases (M-PPases) are homodimeric enzymes that couple the generation and utilization of membrane potentials to pyrophosphate (PPi) hydrolysis and synthesis. Since the discovery of the link between PP; use and proton transport in purple, non-sulphur bacteria in the 1960s, M-PPases have been found in all three domains of life and have been shown to have a crucial role in stress tolerance and in plant maturation. The discovery of sodium-pumping and sodium/proton-pumping M-PPases showed that the pumping specificity of these enzymes is not limited to protons, further suggesting that M-PPases are evolutionarily very ancient. The recent structures of two M-PPases, the Vigna radiata H+-pumping M-PPase and Therm otoga maritima Na+-pumping M-PPase, provide the basis for understanding the functional data. They show that M-PPases have a novel fold and pumping mechanism, different to the other primary pumps. This review discusses the current structural understanding of M-PPases and of ion selection among various M-PPases.
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