3J0J

Fitted atomic models of Thermus thermophilus V-ATPase subunits into cryo-EM map

Summary for 3J0J

• Entry DOI: 10.2210/pdb3j0j/pdb
• EMDB information: 5335
• Descriptor: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (8 entities in total)
• Functional Keywords: flexible fitting, rigid body fitting, membrane protein complex, hydrolase
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 13
• Total formula weight: 488233.98

Authors

Lau, W.C.Y.,Rubinstein, J.L. (deposition date: 2011-08-24, release date: 2011-12-14, Last modification date: 2024-11-20)

Primary citation

Lau, W.C.,Rubinstein, J.L.
Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase.
Nature, 481:214-218, 2012

PubMed Abstract: Ion-translocating rotary ATPases serve either as ATP synthases, using energy from a transmembrane ion motive force to create the cell's supply of ATP, or as transmembrane ion pumps that are powered by ATP hydrolysis. The members of this family of enzymes each contain two rotary motors: one that couples ion translocation to rotation and one that couples rotation to ATP synthesis or hydrolysis. During ATP synthesis, ion translocation through the membrane-bound region of the complex causes rotation of a central rotor that drives conformational changes and ATP synthesis in the catalytic region of the complex. There are no structural models available for the intact membrane region of any ion-translocating rotary ATPase. Here we present a 9.7 Å resolution map of the H(+)-driven ATP synthase from Thermus thermophilus obtained by electron cryomicroscopy of single particles in ice. The 600-kilodalton complex has an overall subunit composition of A(3)B(3)CDE(2)FG(2)IL(12). The membrane-bound motor consists of a ring of L subunits and the carboxy-terminal region of subunit I, which are equivalent to the c and a subunits of most other rotary ATPases, respectively. The map shows that the ring contains 12 L subunits and that the I subunit has eight transmembrane helices. The L(12) ring and I subunit have a surprisingly small contact area in the middle of the membrane, with helices from the I subunit making contacts with two different L subunits. The transmembrane helices of subunit I form bundles that could serve as half-channels across the membrane, with the first half-channel conducting protons from the periplasm to the L(12) ring and the second half-channel conducting protons from the L(12) ring to the cytoplasm. This structure therefore suggests the mechanism by which a transmembrane proton motive force is converted to rotation in rotary ATPases.

PubMed: 22178924
DOI: 10.1038/nature10699

Experimental method

ELECTRON MICROSCOPY (9.7 Å)