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TitleStructural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes.
Journal, issue, pagesStructure, Vol. 15, Issue 12, Page 1674-1683, Year 2007
Publish dateFeb 15, 2008
AuthorsJohan Busselez / Magali Cottevieille / Philippe Cuniasse / Francesca Gubellini / Nicolas Boisset / Daniel Lévy /
PubMed AbstractIn Rhodobacter (Rba.) sphaeroides, the subunit PufX is involved in the dimeric organization of the core complex. Here, we report the 3D reconstruction at 12 A by cryoelectron microscopy of the core ...In Rhodobacter (Rba.) sphaeroides, the subunit PufX is involved in the dimeric organization of the core complex. Here, we report the 3D reconstruction at 12 A by cryoelectron microscopy of the core complex of Rba. veldkampii, a complex of approximately 300 kDa without symmetry. The core complex is monomeric and constituted by a light-harvesting complex 1 (LH1) ring surrounding a uniquely oriented reaction center (RC). The LH1 consists of 15 resolved alpha/beta heterodimers and is interrupted. Within the opening, PufX polypeptide is assigned at a position facing the Q(B) site of the RC. This core complex is different from a dissociated dimer of the core complex of Rba. sphaeroides revealing that PufX in Rba. veldkampii is unable to dimerize. The absence in PufX of Rba. veldkampii of a G(31)XXXG(35) dimerization motif highlights the transmembrane interactions between PufX subunits involved in the dimerization of the core complexes of Rhodobacter species.
External linksStructure / PubMed:18073116
MethodsEM (single particle)
Resolution12.0 Å
Structure data

EMDB-1356:
Structural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes.
Method: EM (single particle) / Resolution: 12.0 Å

Source
  • Rhodobacter veldkampii (bacteria)

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