Structure of plant photosystem I revealed by theoretical modeling

Craig Jolley, Adam Ben-Shem, Nathan Nelson, Petra Fromme

Research output: Contribution to journalArticle

42 Citations (Scopus)

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 languageEnglish
Pages (from-to)33627-33636
Number of pages10
JournalJournal of Biological Chemistry
Volume280
Issue number39
DOIs
Publication statusPublished - Sep 30 2005

Fingerprint

Photosystem I Protein Complex
Plant Structures
X-Rays
Planets
Biological Phenomena
Crystal structure
Structural Models
Peas
Photosynthesis
X rays
Membrane Proteins
Amino Acids

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 journalArticle

Jolley, Craig ; Ben-Shem, Adam ; Nelson, Nathan ; Fromme, Petra. / Structure of plant photosystem I revealed by theoretical modeling. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 39. pp. 33627-33636.
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