5LQX: Structure of F-ATPase from Pichia angusta, state3

Citation:
Abstract
The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane proton motive force across mitochondrial membranes in the synthesis of ATP. This mechanism requires a strong and integral stator, consisting of the catalytic alpha3beta3-domain, peripheral stalk, and, in the membrane domain, subunit a and associated supernumerary subunits, kept in contact with the rotor turning at speeds up to 350 Hz. The stator's integrity is ensured by robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8 subunit provides an additional brace between the peripheral stalk and subunit a. At the junction between the OSCP and the apparently stiff, elongated alpha-helical b-subunit and associated d- and h-subunits, an elbow or joint allows the stator to bend to accommodate lateral movements during the activity of the catalytic domain. The stator may also apply lateral force to help keep the static a-subunit and rotating c10-ring together. The interface between the c10-ring and the a-subunit contains the transmembrane pathway for protons, and their passage across the membrane generates the turning of the rotor. The pathway has two half-channels containing conserved polar residues provided by a bundle of four alpha-helices inclined at approximately 30 degrees to the plane of the membrane, similar to those described in other species. The structure provides more insights into the workings of this amazing machine.
PDB ID: 5LQXDownload
MMDB ID: 158824
PDB Deposition Date: 2016/8/17
Updated in MMDB: 2018/02
Experimental Method:
electron microscopy
Resolution: 7.9  Å
Source Organism:
Ogataea angusta
Similar Structures:
Biological Unit for 5LQX: 30-meric; determined by author
Molecular Components in 5LQX
Label Count Molecule
Proteins (30 molecules)
1
ATP Synthase Subunit F
Molecule annotation
1
ATP Synthase Aap1 Subunit
Molecule annotation
1
ATP Synthase Subunit a
Molecule annotation
1
ATP Synthase Subunit B
Molecule annotation
3
ATP Synthase Alpha Subunit
Molecule annotation
3
ATP Synthase Beta Subunit
Molecule annotation
1
ATP Synthase Gamma Subunit
Molecule annotation
1
ATP Synthase Delta Subunit
Molecule annotation
1
ATP Synthase Epsilon Subunit
Molecule annotation
1
ATP Synthase Inhibitor Protein IF1
Molecule annotation
10
ATP Synthase Subunit C
Molecule annotation
1
ATP Synthase Oscp Subunit
Molecule annotation
1
ATP Synthase Subunit B
Molecule annotation
1
ATP Synthase Subunit D
Molecule annotation
1
ATP Synthase Subunit H
Molecule annotation
1
ATP Synthase Subunit a
Molecule annotation
1
ATP Synthase Subunit a
Molecule annotation
Chemicals (11 molecules)
1
1
2
5
3
5
* Click molecule labels to explore molecular sequence information.

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