2O01 image
Deposition Date 2006-11-27
Release Date 2007-05-08
Last Version Date 2026-08-12
Entry Detail
PDB ID:
2O01
Keywords:
Title:
The Structure of a plant photosystem I supercomplex at 3.4 Angstrom resolution
Biological Source:
Source Organism(s):
Method Details:
Experimental Method:
Resolution:
3.40 Å
R-Value Free:
0.40
R-Value Work:
0.34
R-Value Observed:
0.35
Space Group:
P 1 21 1
Macromolecular Entities
Polymer Type:polypeptide(L)
Molecule:AT3g54890
Gene (Uniprot):LHCA1
Chain IDs:N (auth: 1)
Chain Length:187
Number of Molecules:1
Biological Source:Arabidopsis thaliana
Polymer Type:polypeptide(L)
Molecule:Type II chlorophyll a/b bindi
Gene (Uniprot):lhaB
Chain IDs:O (auth: 2)
Chain Length:186
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:PSI type III chlorophyll a/b-
Gene (Uniprot):LHCA3
Chain IDs:P (auth: 3)
Chain Length:165
Number of Molecules:1
Biological Source:Arabidopsis thaliana
Polymer Type:polypeptide(L)
Molecule:PSI light-harvesting antenna
Gene (Uniprot):lhcA-P4
Chain IDs:Q (auth: 4)
Chain Length:165
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:Photosystem I P700 chlorophyl
Gene (Uniprot):psaA
Chain IDs:A
Chain Length:754
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:Photosystem I P700 chlorophyl
Gene (Uniprot):psaB
Chain IDs:B
Chain Length:732
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:Photosystem I iron-sulfur cen
Gene (Uniprot):psaC
Chain IDs:C
Chain Length:80
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):psaD
Chain IDs:D
Chain Length:138
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):PSAE1
Chain IDs:E
Chain Length:62
Number of Molecules:1
Biological Source:Arabidopsis thaliana
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):PSAF
Chain IDs:F
Chain Length:154
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):PSAG
Chain IDs:G
Chain Length:95
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):PSAH
Chain IDs:H
Chain Length:75
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):psaI
Chain IDs:I
Chain Length:30
Number of Molecules:1
Biological Source:Pisum sativum
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):psaJ
Chain IDs:J
Chain Length:42
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Chain IDs:K
Chain Length:38
Number of Molecules:1
Biological Source:Arabidopsis thaliana
Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):PSAL
Chain IDs:L
Chain Length:164
Number of Molecules:1
Biological Source:Spinacia oleracea
Polymer Type:polypeptide(L)
Molecule:Photosystem I-N subunit
Gene (Uniprot):PSI-N
Chain IDs:M (auth: N)
Chain Length:85
Number of Molecules:1
Biological Source:Phaseolus vulgaris
Primary Citation
The structure of a plant photosystem I supercomplex at 3.4 A resolution.
Nature 447 58 63 (2007)
PMID: 17476261 DOI: 10.1038/nature05687

Abstact

All higher organisms on Earth receive energy directly or indirectly from oxygenic photosynthesis performed by plants, green algae and cyanobacteria. Photosystem I (PSI) is a supercomplex of a reaction centre and light-harvesting complexes. It generates the most negative redox potential in nature, and thus largely determines the global amount of enthalpy in living systems. We report the structure of plant PSI at 3.4 A resolution, revealing 17 protein subunits. PsaN was identified in the luminal side of the supercomplex, and most of the amino acids in the reaction centre were traced. The crystal structure of PSI provides a picture at near atomic detail of 11 out of 12 protein subunits of the reaction centre. At this level, 168 chlorophylls (65 assigned with orientations for Q(x) and Q(y) transition dipole moments), 2 phylloquinones, 3 Fe(4)S(4) clusters and 5 carotenoids are described. This structural information extends the understanding of the most efficient nano-photochemical machine in nature.

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Primary Citation of related structures
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