3ENI

Crystal structure of the Fenna-Matthews-Olson Protein from Chlorobaculum Tepidum

Replaces:  1M50Replaces:  1KSA

Summary for 3ENI

• Entry DOI: 10.2210/pdb3eni/pdb
• Related: 1KSA 1M50 3EOJ
• Descriptor: Bacteriochlorophyll a protein, BACTERIOCHLOROPHYLL A (3 entities in total)
• Functional Keywords: beta sheet, gamma turn, bacteriochlorophyll, chlorophyll, chromophore, electron transport, magnesium, metal-binding, photosynthesis, reaction center, transport
• Biological source: Chlorobaculum tepidum
• Total number of polymer chains: 2
• Total formula weight: 95008.53

Authors

Tronrud, D.,Camara-Artigas, A.,Blankenship, R.,Allen, J.P. (deposition date: 2008-09-25, release date: 2009-05-12, Last modification date: 2024-02-21)

Primary citation

Tronrud, 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

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)