Structure of Plant Photosystem I Revealed by Theoretical Modeling[boxs]

Photosystem (PS) I is a large membrane protein complex vital for oxygenic photosynthesis, one of the most important biological processes on the planet. We present an “atomic” model of higher plant PSI, based on theoretical modeling using the recent 4.4 Å x-ray crystal structure of PSI from pea. Beca...

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Bibliographic Details
Published in:The Journal of biological chemistry 2005-09, Vol.280 (39), p.33627-33636
Main Authors: Jolley, Craig, Ben-Shem, Adam, Nelson, Nathan, Fromme, Petra
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Carotenoids - chemistry
Carotenoids - metabolism
Chlorophyll - chemistry
Chlorophyll - metabolism
Computer Simulation
Conserved Sequence
Crystallography, X-Ray
Cyanobacteria - chemistry
Ferredoxins - chemistry
Ferredoxins - metabolism
Ligands
Light-Harvesting Protein Complexes - chemistry
Light-Harvesting Protein Complexes - metabolism
Lipids - chemistry
Models, Molecular
Models, Theoretical
Molecular Sequence Data
Photosystem I Protein Complex - chemistry
Photosystem I Protein Complex - metabolism
Pisum sativum - chemistry
Plastocyanin - metabolism
Protein Conformation
Protein Structure, Secondary
Protein Subunits - chemistry
Protein Subunits - metabolism
Sequence Homology, Amino Acid
Static Electricity
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Summary:Photosystem (PS) I is a large membrane protein complex vital for oxygenic photosynthesis, one of the most important biological processes on the planet. We present an “atomic” model of higher plant PSI, based on theoretical modeling using the recent 4.4 Å x-ray crystal structure of PSI from pea. Because of the lack of information on the amino acid side chains in the x-ray structural model and the high cofactor content in this system, novel modeling techniques were developed. Our model reveals some important structural features of plant PSI that were not visible in the crystal structure, and our model sheds light on the evolutionary relationship between plant and cyanobacterial PSI.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M500937200