TY - JOUR
T1 - Structure of the dimeric RC-LH1-PufX complex from Rhodobaca bogoriensis investigated by electron microscopy
AU - Semchonok, D.A.
AU - Chauvin, J.P.
AU - Frese, R.N.
AU - Jungas, C.
AU - Boekema, E.J.
PY - 2012
Y1 - 2012
N2 - Electron microscopy and single-particle averaging were performed on isolated reaction centre (RC)- antenna complexes (RC-LH1-PufX complexes) of Rhodobaca bogoriensis strain LBB1, with the aimof establishing the LH1 antenna conformation, and, in particular, the structural role of the PufX protein. Projection maps of dimeric complexes were obtained at 13Å resolution and show the positions of the 2 × 14 LH1 α- and β-subunits. This new dimeric complex displays two open, C-shaped LH1 aggregates of 13 αβ polypeptides partially surrounding the RCs plus two LH1 units forming the dimer interface in the centre. Between the interface and the two half rings are two openings on each side. Next to the openings, there are four additional densities present per dimer, considered to be occupied by four copies of PufX. The position of the RC in our model was verified by comparison with RC- LH1-PufX complexes in membranes. Our model differs from previously proposed configurations for Rhodobacter species in which the LH1 ribbon is continuous in the shape of an S, and the stoichiometry is of one PufX per RC. © 2012 The Royal Society.
AB - Electron microscopy and single-particle averaging were performed on isolated reaction centre (RC)- antenna complexes (RC-LH1-PufX complexes) of Rhodobaca bogoriensis strain LBB1, with the aimof establishing the LH1 antenna conformation, and, in particular, the structural role of the PufX protein. Projection maps of dimeric complexes were obtained at 13Å resolution and show the positions of the 2 × 14 LH1 α- and β-subunits. This new dimeric complex displays two open, C-shaped LH1 aggregates of 13 αβ polypeptides partially surrounding the RCs plus two LH1 units forming the dimer interface in the centre. Between the interface and the two half rings are two openings on each side. Next to the openings, there are four additional densities present per dimer, considered to be occupied by four copies of PufX. The position of the RC in our model was verified by comparison with RC- LH1-PufX complexes in membranes. Our model differs from previously proposed configurations for Rhodobacter species in which the LH1 ribbon is continuous in the shape of an S, and the stoichiometry is of one PufX per RC. © 2012 The Royal Society.
U2 - 10.1098/rstb.2012.0063
DO - 10.1098/rstb.2012.0063
M3 - Article
SN - 0962-8436
VL - 367
SP - 3412
EP - 3419
JO - Philosophical Transactions of the Royal Society B. Biological Sciences
JF - Philosophical Transactions of the Royal Society B. Biological Sciences
IS - 1608
ER -