1IZL

Crystal Structure of Photosystem II

Summary for 1IZL

• Entry DOI: 10.2210/pdb1izl/pdb
• Related: 1FE1 1ILX
• Descriptor: Photosystem II: Subunit PsbA, Photosystem II: Subunit PsbK, Photosystem II: Subunit PsbO, ... (21 entities in total)
• Functional Keywords: photosynthesis, photosynthetic reaction center, core-antenna, thermophilic cyanobacterium, membrane protein complex, electron transfer, energy transfer
• Biological source: Thermosynechococcus vulcanus; More
• Total number of polymer chains: 28
• Total formula weight: 600355.53

Authors

Kamiya, N.,Shen, J.-R. (deposition date: 2002-10-04, release date: 2003-01-14, Last modification date: 2023-12-27)

Primary citation

Kamiya, N.,Shen, J.-R.
Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution
Proc.Natl.Acad.Sci.USA, 100:98-103, 2003

PubMed Abstract: Photosystem II (PSII) is a multisubunit membrane protein complex performing light-induced electron transfer and water-splitting reactions, leading to the formation of molecular oxygen. The first crystal structure of PSII from a thermophilic cyanobacterium Thermosynechococcus elongatus was reported recently [Zouni, A., Witt, H. T., Kern, J., Fromme, P., Krauss, N., Saenger, W. & Orth, P. (2001) Nature 409, 739-743)] at 3.8-A resolution. To analyze the PSII structure in more detail, we have obtained the crystal structure of PSII from another thermophilic cyanobacterium, Thermosynechococcus vulcanus, at 3.7-A resolution. The present structure was built on the basis of the sequences of PSII large subunits D1, D2, CP47, and CP43; extrinsic 33- and 12-kDa proteins and cytochrome c550; and several low molecular mass subunits, among which the structure of the 12-kDa protein was not reported previously. This yielded much information concerning the molecular interactions within this large protein complex. We also show the arrangement of chlorophylls and cofactors, including two beta-carotenes recently identified in a region close to the reaction center, which provided important clues to the secondary electron transfer pathways around the reaction center. Furthermore, possible ligands for the Mn-cluster were determined. In particular, the C terminus of D1 polypeptide was shown to be connected to the Mn cluster directly. The structural information obtained here provides important insights into the mechanism of PSII reactions.

PubMed: 12518057
DOI: 10.1073/pnas.0135651100

Experimental method

X-RAY DIFFRACTION (3.7 Å)