Structural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes

被引：23

作者：

Busselez, Johan ^{[1
]}

Cottevieille, Magali ^{[2
]}

Cuniasse, Philippe ^{[3
]}

Gubellini, Francesca ^{[1
]}

Boisset, Nicolas ^{[2
]}

Levy, Daniel ^{[1
]}

机构：

[1] Inst Curie, CNRS, UMR 168, F-75231 Paris, France

[2] CNRS, IMPMC, UMR 7590, F-75005 Paris, France

[3] CEA, iBiTecS, SIMOPRO, LCV, F-91191 Gif Sur Yvette, France

来源：

STRUCTURE | 2007年 / 15卷 / 12期

关键词：

D O I：

10.1016/j.str.2007.09.026

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom by cryoelectron microscopy of the core complex of Rba. veldkampii, a complex of similar to 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 dimenze. 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.

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页码：1674 / 1683

页数：10

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