TY - JOUR
T1 - Crystallographic refinement at 2.3 Å resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis
AU - Deisenhofer, Johann
AU - Epp, Otto
AU - Sinning, Irmgard
AU - Michel, Hartmut
N1 - Funding Information:
We thank Dr. U. Errnler and C. R. D. Lancaster for reading the manuscript, Dorothee Staber for assistance with preparation of the manuscript, and Diana Diggs for help with Figure 4. This work was supported by the Max-Planck-Gesellschaft, the Deutsche Forschungsge-meinschaft (SFB 143), and the Fonds der Chemischen Industrie.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1995/2/24
Y1 - 1995/2/24
N2 - The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 Å resolution. The refined model contains 10,288 non-hydrogen atoms; 10,045 of these have well defined electron density. A Luzzati-plot indicates an average co-ordinate error of 0.26 Å. During refinement, the positions of a partially ordered carotenoid, a unibiquinone in the partially occupied QB site, a detergent molecule, seven putative sulphate ions, and 201 water molecules were found. More than half of these waters are bound at interfaces between protein subunits and therefore contribute significantly to subunit interactions. Water molecules also play important structural and probably functional roles in the environment of some of the cofactors. Two water molecules form hydrogen bonds to the accessory bacteriochlorophylls and to the protein in the vicinity of the special pair of bacteriophylls, the primary electron donor. A group of about 10 water molecules is bound near the binding site of the secondary quinone QB. These waters are likely to participate in the transfer of protons to the doubly reduced QB.
AB - The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 Å resolution. The refined model contains 10,288 non-hydrogen atoms; 10,045 of these have well defined electron density. A Luzzati-plot indicates an average co-ordinate error of 0.26 Å. During refinement, the positions of a partially ordered carotenoid, a unibiquinone in the partially occupied QB site, a detergent molecule, seven putative sulphate ions, and 201 water molecules were found. More than half of these waters are bound at interfaces between protein subunits and therefore contribute significantly to subunit interactions. Water molecules also play important structural and probably functional roles in the environment of some of the cofactors. Two water molecules form hydrogen bonds to the accessory bacteriochlorophylls and to the protein in the vicinity of the special pair of bacteriophylls, the primary electron donor. A group of about 10 water molecules is bound near the binding site of the secondary quinone QB. These waters are likely to participate in the transfer of protons to the doubly reduced QB.
KW - Cofactor interactions
KW - Crystal structure
KW - Membrane protein
KW - Photosynthetic reaction centre
KW - Subunit interactions
UR - http://www.scopus.com/inward/record.url?scp=0028957690&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028957690&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1994.0097
DO - 10.1006/jmbi.1994.0097
M3 - Article
C2 - 7877166
AN - SCOPUS:0028957690
SN - 0022-2836
VL - 246
SP - 429
EP - 457
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -