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Fmo protein from Prosthecochloris Aestuarii 2K AT 1.3A ResolutionFmo protein from Prosthecochloris Aestuarii 2K AT 1.3A Resolution
Structural highlights
FunctionBCPA_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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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