3V3C: Crystal Structure Of Chloroplast Atp Synthase C-ring From Pisum Sativum

A ring of 8-15 identical c-subunits is essential for ion-translocation by the rotary electromotor of the ubiquitous F(O)F(1)-ATPase. Here we present the crystal structure at 3.4A resolution of the c-ring from chloroplasts of a higher plant (Pisum sativum), determined using a native preparation. The crystal structure was found to resemble that of an (ancestral) cyanobacterium. Using elastic network modeling to investigate the ring's eigen-modes, we found five dominant modes of motion that fell into three classes. They revealed the following deformations of the ring: (I) ellipsoidal, (II) opposite twisting of the luminal circular surface of the ring against the stromal surface, and (III) kinking of the hairpin-shaped monomers in the middle, resulting in bending/stretching of the ring. Extension of the elastic network analysis to rings of different c(n)-symmetry revealed the same classes of dominant modes as in P. sativum (c(14)). We suggest the following functional roles for these classes: The first and third classes of modes affect the interaction of the c-ring with its counterparts in F(O), namely subunits a and bb'. These modes are likely to be involved in ion-translocation and torque generation. The second class of deformation, along with deformations of subunits gamma and epsilon might serve to elastically buffer the torque transmission between F(O) and F(1).
PDB ID: 3V3CDownload
MMDB ID: 103466
PDB Deposition Date: 2011/12/13
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 3.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3V3C: tetradecameric; determined by author
Molecular Components in 3V3C
Label Count Molecule
Proteins (14 molecules)
ATP Synthase Subunit C, Chloroplastic(Gene symbol: atpH)
Molecule annotation
Chemicals (25 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB