3eoj

Fmo protein from Prosthecochloris Aestuarii 2K AT 1.3A Resolution

spinqualitylabelsall models 3eoj, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3eoj is a 1 chain structure with sequence from Dsm 271. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCL, EDO, NA, NH4 Related: 4bcl, 3bcl, 2bcl, 1bcl, 3eni Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BCPA_PROAE] Intermediary in the transfer of excitation energy from the chlorophyll to the reaction centers. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The absorbance spectrum of the Fenna-Matthews-Olson protein--a component of the antenna system of Green Sulfur Bacteria--is always one of two types, depending on the species of the source organism. The FMO from Prosthecochloris aestuarii 2K has a spectrum of type 1 while that from Chlorobaculum tepidum is of type 2. The previously reported crystal structures for these two proteins did not disclose any rationale that would explain their spectral differences. We have collected a 1.3 A X-ray diffraction dataset of the FMO from Prosthecochloris aestuarii 2K, which has allowed us to identify an additional Bacteriochlorophyll-a molecule with chemical attachments to both sides of the central magnesium atom. A new analysis of the previously published X-ray data for the Chlorobaculum tepidum FMO shows the presence of a Bacteriochlorophyll-a molecule in an equivalent location but with a chemical attachment from only one side. This difference in binding is shown to be predictive of the spectral type of the FMO. The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria.,Tronrud DE, Wen J, Gay L, Blankenship RE Photosynth Res. 2009 May;100(2):79-87. Epub 2009 May 13. PMID:19437128 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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