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The structural basis for the difference in absorbance spectra for the FMO antenna protein from various green sulfur bacteria

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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 Å 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.

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Abbreviations

Bchl-a :

Bacteriochlorophyll-a

Cbl :

Chlorobaculum

FMO:

Fenna–Matthews–Olson Protein

PDB:

Protein Data Bank

Pel :

Pelodictyon

Ptc :

Prosthecochloris

r.m.s.:

Root mean square

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Acknowledgments

The authors would like to thank a number of individuals for their assistance and advice in performing this work. Roger Fenna provided advice on the purification and crystallization of this protein that was helpful in recreating the crystal form he had used in his earlier work. George Sheldrick answered a great many questions about the operation of his program ShelxL. Tom Terwilliger helped out with the operation of his Phenix.AutoBuild program. Tom Womack, Clemens Vonrhein, and others at Global Phasing, Ltd helped with the operation of AutoBuster. Anthony Addlagatta provided advice and assistance in crystal handling and data collection. X-ray diffraction data were collected at ALS beamline 8.2.2. Figures 1, 2 and 3 were created using the program PyMOL (http://www.pymol.org/). R. E. Blankenship gratefully acknowledges support from grant #DE-FG02-07ER15846 from the Energy Biosciences program of the Basic Energy Sciences division of the US Department of Energy. D. E. Tronrud wishes to thank B. W. Matthews for agreeing to host this project in his lab.

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  1. Dale E. Tronrud

    Present address: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, 97331, USA

Authors and Affiliations

  1. Howard Hughes Medical Institute, Institute of Molecular Biology, University of Oregon, Eugene, OR, 97403, USA

    Dale E. Tronrud & Leslie Gay

  2. Departments of Biology and Chemistry, Washington University, St Louis, MO, 63130, USA

    Jianzhong Wen & Robert E. Blankenship

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  1. Dale E. Tronrud
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Correspondence to Dale E. Tronrud.

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Tronrud, D.E., Wen, J., Gay, L. et al. 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). https://doi.org/10.1007/s11120-009-9430-6

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