Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 326, Issue 5, Pages 1523-1538Publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(03)00024-X
Keywords
light-harvesting; TLS refinement; X-ray structure; carotenoid; energy transfer
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The structure at 100 K of integral membrane light-harvesting complex 11 (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to 2.0 Angstrom resolution. The plectron density has been significantly improved, compared to the 2.5 Angstrom resolution map, by high resolution data, cryo-cooling and translation, libration, screw (TLS) refinement. The electron density reveals a second carotenoid molecule, the last five C-terminal residues of the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand of the B800 bacteriochlorophyll. TLS refinement has enabled the characterisation of displacements between molecules in the complex. B850 bacteriochlorophyll molecules are arranged in a ring of 18 pigments composed of nine approximate dimers. These pigments are strongly coupled and at their equilibrium positions the excited state dipole interaction energies, within and between dimers, are similar to370 cm(-1) and 280 cm(-1), respectively. This difference in coupling energy is similar in magnitude to changes in interaction energies arising from the pigment displacements described by TLS tensors. The displacements appear to be non-random in nature and appear to be designed to optimise the modulation of pigment energy interactions. This is the first time that LH2 pigment displacements have been quantified experimentally. The calculated energy changes indicate that there may be significant contributions to inter-pigment energy interactions from molecular displacements and these may be of importance to photosynthetic energy transfer. (C) 2003 Elsevier Science Ltd. All rights reserved.
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