4AV3

Crystal structure of Thermotoga Maritima sodium pumping membrane integral pyrophosphatase with metal ions in active site

Summary for 4AV3

• Entry DOI: 10.2210/pdb4av3/pdb
• Related: 4AV6
• Descriptor: K(+)-STIMULATED PYROPHOSPHATE-ENERGIZED SODIUM PUMP, MAGNESIUM ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, membrane pyrophosphotase, ion pump
• Biological source: THERMOTOGA MARITIMA
• Cellular location: Cell membrane ; Multi-pass membrane protein : Q9S5X0
• Total number of polymer chains: 2
• Total formula weight: 156563.05

Authors

Kajander, T.,Kogan, K.,Kellosalo, J.,Pokharel, K.,Goldman, A. (deposition date: 2012-05-23, release date: 2012-08-08, Last modification date: 2024-05-01)

Primary citation

Kellosalo, J.,Kajander, T.,Kogan, K.,Pokharel, K.,Goldman, A.
The Structure and Catalytic Cycle of a Sodium-Pumping Pyrophosphatase.
Science, 337:473-, 2012

PubMed Abstract: 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 α 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.

PubMed: 22837527
DOI: 10.1126/SCIENCE.1222505

Experimental method

X-RAY DIFFRACTION (2.6 Å)