caa a22 4500 445889853 CHVBK 20180317145612.0 cr unu---uuuuu 170323e20110201xx s 000 0 eng 10.1007/s11120-010-9604-2 doi (NATIONALLICENCE)springer-10.1007/s11120-010-9604-2 The three-dimensional structure of the FMO protein from Pelodictyon phaeum and the implications for energy transfer [Elektronische Daten] [Chadwick Larson, Chenda Seng, Lisa Lauman, Heather Matthies, Jianzhong Wen, Robert Blankenship, James Allen] The Fenna-Matthews-Olson (FMO) antenna protein from the green bacterium Pelodictyon phaeum mediates the transfer of energy from the peripheral chlorosome antenna complex to the membrane-bound reaction center. The three-dimensional structure of this protein has been solved using protein crystallography to a resolution limit of 2.0Å, with R work and R free values of 16.6 and 19.9%, respectively. The structure is a trimer of three identical subunits related by a threefold symmetry axis. Each subunit has two beta sheets that surround 8 bacteriochlorophylls. The bacteriochlorophylls are all five-coordinated, with the axial ligand being a histidine, serine, backbone carbonyl, or bound water molecule. The arrangement of the bacteriochlorophylls is generally well conserved in comparison to other FMO structures, but differences are apparent in the interactions with the surrounding protein. In this structure the position and orientation of the eighth bacteriochlorophyll is well defined and shows differences in its location and the coordination of the central Mg compared to previous models. The implications of this structure on the ability of the FMO protein to perform energy transfer are discussed in terms of the experimental optical measurements. Springer Science+Business Media B.V., 2010 Light-harvesting complex nationallicence Green bacteria nationallicence Photosynthesis nationallicence Energy transfer nationallicence Chlorosome nationallicence FMO : Fenna-Matthews-Olson nationallicence BChl a : Bacteriochlorophyll a nationallicence Larson Chadwick Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut Seng Chenda Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut Lauman Lisa Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut Matthies Heather Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut Wen Jianzhong Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut Blankenship Robert Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut Allen James Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut Photosynthesis Research Springer Netherlands 107/2(2011-02-01), 139-150 0166-8595 107:2<139 2011 107 11120 https://doi.org/10.1007/s11120-010-9604-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11120-010-9604-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Larson Chadwick Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut NATIONALLICENCE 700 1- Seng Chenda Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut NATIONALLICENCE 700 1- Lauman Lisa Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut NATIONALLICENCE 700 1- Matthies Heather Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut NATIONALLICENCE 700 1- Wen Jianzhong Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut NATIONALLICENCE 700 1- Blankenship Robert Departments of Biology and Chemistry, Washington University in St. Louis, 63130, St. Louis, MO, USA aut NATIONALLICENCE 700 1- Allen James Department of Chemistry and Biochemistry, Arizona State University, 85287-1604, Tempe, AZ, USA aut NATIONALLICENCE 773 0- Photosynthesis Research Springer Netherlands 107/2(2011-02-01), 139-150 0166-8595 107:2<139 2011 107 11120 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer