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  Cyanobacterial photosystem II at 3.2 A resolution - the plastoquinone binding pockets

Kern, J., Loll, B., Zouni, A., Irrgang, K., Saenger, W., & Biesiadka, J. (2005). Cyanobacterial photosystem II at 3.2 A resolution - the plastoquinone binding pockets. Photosynthesis Research, 84(1), 153-159. doi:10.1007/s11120-004-7077-x.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-4FFB-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-4FFC-B
Genre: Journal Article
Alternative Title : Cyanobacterial Photosystem II at 3.2 Å resolution - the plastoquinone binding pockets

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PhotosynthRes_84_2005_153.pdf (Any fulltext), 317KB
 
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 Creators:
Kern, Jana1, Author              
Loll, Bernhard2, Author              
Zouni, Athina, Author
Irrgang, Klaus−Dieter, Author
Saenger, Wolfram, Author
Biesiadka, Jacek, Author
Affiliations:
1Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: crystal structure, Photosystem II, plastoquinone 9, quinone binding sites, Thermosynechococcus elongatus
 Abstract: Photosystem II from thylakoid membranes of the thermophilic cyanobacterium Thermosynechococcus elongatus was solubilized with n-beta-dodecylmaltoside and purified using anion exchange chromatography. Molecular weight, pigment stoichiometry and subunit composition were assayed using various techniques. The holocomplex is dimeric with a molecular mass of 756 +/- 18 kDa and functionally fully active. Crystals obtained from these samples showed significantly improved quality leading to a 3D structure at 3.2 A resolution. Several loop regions of the principal protein subunits are now defined that were not interpretable at lower (3.8 A) resolution, thus resulting in a more complete model. The head groups of the cofactors of the electron transfer chain and of the antennae have been modeled, coordinating and hydrogen bonding amino acids identified and the nature of the binding pockets derived. The orientations of these cofactors resemble those of the reaction centre from anoxygenic purple bacteria. For the two plastoquinones, electron density was only found for the head group of QA and none for QB indicating low or even no occupancy of this site in the crystal structure. Both binding pockets and problems related to the QB site are discussed here and compared to the situation in the purple bacterial reaction centre.

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Language(s): eng - English
 Dates: 2004-09-292004-12-022005-06-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Photosynthesis Research
Source Genre: Journal
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Publ. Info: Hague : W. Junk
Pages: - Volume / Issue: 84 (1) Sequence Number: - Start / End Page: 153 - 159 Identifier: ISSN: 0166-8595
CoNE: https://pure.mpg.de/cone/journals/resource/954925482637