Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.5
Classification:PHOTOSYNTHESIS
Release Date:2001-08-01
Deposition Date:2001-06-01
Revision Date:2008-04-27#2011-07-13#2012-07-25#2016-05-11#2018-01-24
Molecular Weight:359700.12
Macromolecule Type:Protein
Residue Count:2334
Atom Site Count:23997
DOI:10.2210/pdb1jb0/pdb
Abstract:
Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved.
Resolution:2.5
Classification:PHOTOSYNTHESIS
Release Date:2001-08-01
Deposition Date:2001-06-01
Revision Date:2008-04-27#2011-07-13#2012-07-25#2016-05-11#2018-01-24
Molecular Weight:359700.12
Macromolecule Type:Protein
Residue Count:2334
Atom Site Count:23997
DOI:10.2210/pdb1jb0/pdb
Abstract:
Life on Earth depends on photosynthesis, the conversion of light energy from the Sun to chemical energy. In plants, green algae and cyanobacteria, this process is driven by the cooperation of two large protein-cofactor complexes, photosystems I and II, which are located in the thylakoid photosynthetic membranes. The crystal structure of photosystem I from the thermophilic cyanobacterium Synechococcus elongatus described here provides a picture at atomic detail of 12 protein subunits and 127 cofactors comprising 96 chlorophylls, 2 phylloquinones, 3 Fe4S4 clusters, 22 carotenoids, 4 lipids, a putative Ca2+ ion and 201 water molecules. The structural information on the proteins and cofactors and their interactions provides a basis for understanding how the high efficiency of photosystem I in light capturing and electron transfer is achieved.
| Date made available | Aug 1 2001 |
|---|---|
| Publisher | RCSB-PDB |