Journal
SCIENCE
Volume 337, Issue 6093, Pages 473-476Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1222505
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Funding
- European Union Seventh Framework Program EDICT
- Sigrid Juselius Foundation
- Academy of Finland
- Biocenter Finland
- National Graduate School of Informational and Structural Biology
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Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na+ or H+ pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual coupling funnel of six a helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.
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