3V3C
Crystal Structure of Chloroplast ATP synthase c-ring from Pisum sativum
Summary for 3V3C
| Entry DOI | 10.2210/pdb3v3c/pdb |
| Descriptor | ATP synthase subunit c, chloroplastic, DIGALACTOSYL DIACYL GLYCEROL (DGDG), YTTRIUM (III) ION, ... (4 entities in total) |
| Functional Keywords | c-ring, proton translocation, photosynthesis, proton binding |
| Biological source | Pisum sativum (garden pea,peas) |
| Cellular location | Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein: P08212 |
| Total number of polymer chains | 14 |
| Total formula weight | 111221.68 |
| Authors | Saroussi, S.,Nelson, N. (deposition date: 2011-12-13, release date: 2012-10-03, Last modification date: 2024-02-28) |
| Primary citation | Saroussi, S.,Schushan, M.,Ben-Tal, N.,Junge, W.,Nelson, N. Structure and flexibility of the C-ring in the electromotor of rotary F(o)F(1)-ATPase of pea chloroplasts. Plos One, 7:e43045-e43045, 2012 Cited by PubMed Abstract: 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 3.4Å 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 γ and ε might serve to elastically buffer the torque transmission between F(O) and F(1). PubMed: 23049735DOI: 10.1371/journal.pone.0043045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.402 Å) |
Structure validation
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