2RCR

STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES

Summary for 2RCR

• Entry DOI: 10.2210/pdb2rcr/pdb
• Descriptor: PHOTOSYNTHETIC REACTION CENTER (L SUBUNIT), PHOTOSYNTHETIC REACTION CENTER (M SUBUNIT), PHOTOSYNTHETIC REACTION CENTER (H SUBUNIT), ... (7 entities in total)
• Functional Keywords: photosynthetic reaction center
• Biological source: Rhodobacter sphaeroides; More
• Cellular location: Cellular chromatophore membrane; Multi-pass membrane protein: P02954 P02953; Cellular chromatophore membrane; Single-pass membrane protein: P11846
• Total number of polymer chains: 3
• Total formula weight: 101018.23

Authors

Chang, C.-H.,Norris, J.,Schiffer, M. (deposition date: 1991-02-04, release date: 1993-07-15, Last modification date: 2024-02-21)

Primary citation

Chang, C.H.,el-Kabbani, O.,Tiede, D.,Norris, J.,Schiffer, M.
Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.
Biochemistry, 30:5352-5360, 1991

PubMed Abstract: The structure of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides was determined at 3.1-A resolution by the molecular replacement method, using the Rhodopseudomonas viridis RC as the search structure. Atomic coordinates were refined with the difference Fourier method and restrained least-squares refinement techniques to a current R factor of 22%. The tertiary structure of the RC complex is stabilized by hydrophobic interactions between the L and M chains, by interactions of the pigments with each other and with the L and M chains, by residues from the L and M chains that coordinate to the Fe2+, by salt bridges that are formed between the L and M chains and the H chain, and possibly by electrostatic forces between the ends of helices. The conserved residues at the N-termini of the L and M chains were identified as recognition sites for the H chain.

PubMed: 2036404
DOI: 10.1021/bi00236a005

Experimental method

X-RAY DIFFRACTION (3.1 Å)