Crystal structure of plant photosystem I

Adam Ben-Shem, Felix Frolow, Nathan Nelson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

693 Scopus citations

Abstract

Oxygenic photosynthesis is the principal producer of both oxygen and organic matter on Earth. The conversion of sunlight into chemical energy is driven by two multisubunit membrane protein complexes named photosystem I and II. We determined the crystal structure of the complete photosystem I (PSI) from a higher plant (Pisum sativum var. alaska) to 4.4Å resolution. Its intricate structure shows 12 core subunits, 4 different light-harvesting membrane proteins (LHCI) assembled in a half-moon shape on one side of the core, 45 transmembrane helices, 167 chlorophylls, 3 Fe-S clusters and 2 phylloquinones. About 20 chlorophylls are positioned in strategic locations in the cleft between LHCI and the core. This structure provides a framework for exploration not only of energy and electron transfer but also of the evolutionary forces that shaped the photosynthetic apparatus of terrestrial plants after the divergence of chloroplasts from marine cyanobacteria one billion years ago.

Original languageEnglish
Pages (from-to)630-635
Number of pages6
JournalNature
Volume426
Issue number6967
DOIs
StatePublished - 11 Dec 2003

Funding

FundersFunder number
Israel Science Foundation

    Fingerprint

    Dive into the research topics of 'Crystal structure of plant photosystem I'. Together they form a unique fingerprint.

    Cite this