3vdi

Structure of the FMO protein from Pelodictyon phaeum

spinqualitylabelsall models 3vdi, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vdi is a 1 chain structure with sequence from Pelodictyon phaeum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.99Å Ligands: PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A, 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 beta-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. Reinterpretation of the electron density at the site of the eighth bacteriochlorophyll in the FMO protein from Pelodictyon phaeum.,Tronrud DE, Allen JP Photosynth Res. 2012 Mar 29. PMID:22457093 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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