Abstract
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 2.0 Å, with Rwork and Rfree 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 139-150 |
| Number of pages | 12 |
| Journal | Photosynthesis Research |
| Volume | 107 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 2011 |
Fingerprint
Keywords
- Chlorosome
- Energy transfer
- Green bacteria
- Light-harvesting complex
- Photosynthesis
ASJC Scopus subject areas
- Plant Science
- Cell Biology
- Biochemistry
Cite this
The three-dimensional structure of the FMO protein from Pelodictyon phaeum and the implications for energy transfer. / Larson, Chadwick R.; Seng, Chenda O.; Lauman, Lisa; Matthies, Heather J.; Wen, Jianzhong; Blankenship, Robert E.; Allen, James.
In: Photosynthesis Research, Vol. 107, No. 2, 02.2011, p. 139-150.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The three-dimensional structure of the FMO protein from Pelodictyon phaeum and the implications for energy transfer
AU - Larson, Chadwick R.
AU - Seng, Chenda O.
AU - Lauman, Lisa
AU - Matthies, Heather J.
AU - Wen, Jianzhong
AU - Blankenship, Robert E.
AU - Allen, James
PY - 2011/2
Y1 - 2011/2
N2 - 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 2.0 Å, with Rwork and Rfree 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.
AB - 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 2.0 Å, with Rwork and Rfree 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.
KW - Chlorosome
KW - Energy transfer
KW - Green bacteria
KW - Light-harvesting complex
KW - Photosynthesis
UR - http://www.scopus.com/inward/record.url?scp=79953844961&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79953844961&partnerID=8YFLogxK
U2 - 10.1007/s11120-010-9604-2
DO - 10.1007/s11120-010-9604-2
M3 - Article
C2 - 21181557
AN - SCOPUS:79953844961
VL - 107
SP - 139
EP - 150
JO - Photosynthesis Research
JF - Photosynthesis Research
SN - 0166-8595
IS - 2
ER -