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3EOJ

Fmo protein from Prosthecochloris Aestuarii 2K AT 1.3A Resolution

Summary for 3EOJ
Entry DOI10.2210/pdb3eoj/pdb
Related1BCL 2BCL 3BCL 3ENI 4BCL
DescriptorBacteriochlorophyll a protein, BACTERIOCHLOROPHYLL A, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordsexcitation energy transfer, beta sheet, gamma-turns, bacteriochlorophyll, chlorophyll, chromophore, electron transport, magnesium, metal-binding, photosynthesis, reaction center, transport
Biological sourceProsthecochloris aestuarii 2K
Total number of polymer chains1
Total formula weight48546.25
Authors
Tronrud, D.E.,Wen, J.,Gay, L.,Blankenship, R.E. (deposition date: 2008-09-27, release date: 2009-05-12, Last modification date: 2023-09-06)
Primary citationTronrud, D.E.,Wen, J.,Gay, L.,Blankenship, R.E.
The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria.
Photosynth.Res., 100:79-87, 2009
Cited by
PubMed Abstract: 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.
PubMed: 19437128
DOI: 10.1007/s11120-009-9430-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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