Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 33627-33636 |
| Number of pages | 10 |
| Journal | Journal of Biological Chemistry |
| Volume | 280 |
| Issue number | 39 |
| DOIs | |
| State | Published - Sep 30 2005 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Structure of plant photosystem I revealed by theoretical modeling. / Jolley, Craig; Ben-Shem, Adam; Nelson, Nathan; Fromme, Petra.
In: Journal of Biological Chemistry, Vol. 280, No. 39, 30.09.2005, p. 33627-33636.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Structure of plant photosystem I revealed by theoretical modeling
AU - Jolley, Craig
AU - Ben-Shem, Adam
AU - Nelson, Nathan
AU - Fromme, Petra
PY - 2005/9/30
Y1 - 2005/9/30
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=24144441812&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=24144441812&partnerID=8YFLogxK
U2 - 10.1074/jbc.M500937200
DO - 10.1074/jbc.M500937200
M3 - Article
C2 - 15955818
AN - SCOPUS:24144441812
VL - 280
SP - 33627
EP - 33636
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 39
ER -