Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits.
The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of 2.8 A with an R factor of 26%. The L and M subunits each contain five transmembrane helices and several helices that do not span the membrane. The L and M subunits are related to each other by a 2-fold rotational symmetry axis that is approximately the same as that determined for the cofactors. The H subunit has one transmembrane helix and a globular domain on the cytoplasmic side, which contains a helix that does not span the membrane and several beta-sheets. The structural homology with RCs from other purple bacteria is discussed. A structure of the complex formed between the water soluble cytochrome c2 and the RC from Rb. sphaeroides is proposed.
Allen
J P
JP
Feher
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G
Yeates
T O
TO
Komiya
H
H
Rees
D C
DC
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D045362:Cytochromes c2; D008958:Models, Molecular; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides; D013045:Species Specificity
D001426:Bacterial Proteins; D003574:Cytochrome c Group; D045322:Photosynthetic Reaction Center Complex Proteins; D045362:Cytochromes c2