3VDI

Structure of the FMO protein from Pelodictyon phaeum

Replaces:  3OEG

Summary for 3VDI

• Entry DOI: 10.2210/pdb3vdi/pdb
• Related: 3ENI 3EOJ
• Descriptor: bacteriochlorophyll A protein, BACTERIOCHLOROPHYLL A, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: alpha/beta protein, energy transfer, photosynthesis
• Biological source: Pelodictyon phaeum (green sulfur bacteria)
• Total number of polymer chains: 1
• Total formula weight: 47777.18

Authors

Tronrud, D.E.,Larson, C.R.,Seng, C.O.,Lauman, L.,Matthies, H.J.,Wen, J.,Blankenship, R.E.,Allen, J.P. (deposition date: 2012-01-05, release date: 2012-01-25, Last modification date: 2023-09-13)

Primary citation

Tronrud, D.E.,Allen, J.P.
Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum.
Photosynth.Res., 112:71-74, 2012

PubMed Abstract: The Fenna-Matthews-Olson antenna protein from the green bacterium Pelodictyon phaeum mediates the energy transfer from a peripheral antenna complex to the membrane-bound reaction center. The three-dimensional structure of this protein has been previously modeled using X-ray diffraction to a resolution limit of 2.0 Å, with R (work) and R (free) values of 16.6 and 19.9%, respectively (Larson et al., Photosynth Res 107:139-150, 2011). This model shows the protein as consisting of β-sheets surrounding several bacteriochlorophyll cofactors. While most of the model clearly matches the electron density maps, in this paper we re-examine the electron density for a specific feature, namely the eighth bacteriochlorophyll a cofactor. This electron density is now interpreted as arising primarily from the end of an otherwise disordered polyethylene glycol molecule. Additional electron density is present but the density is weak and cannot be unambiguously assigned. The new model has R (work) and R (free) values of 16.2 and 19.0%, respectively.

PubMed: 22457093
DOI: 10.1007/s11120-012-9735-8

Experimental method

X-RAY DIFFRACTION (1.99 Å)