Photosystem II: Difference between revisions
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[[Image:1s5l.gif|250px|left]] | [[Image:1s5l.gif|250px|left]] | ||
==Background== | ==Background== | ||
This structure of Photosystem II was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>Loll, B., Kern, J., Saenger, W., Zouni, A., Biesiadka, J. "Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II." Nature 2005, 438: 1040-1044. PMID: [http://www.ncbi.nlm.nih.gov/pubmed/16355230 16355230]</ref> and at 3.50 Å | This structure of Photosystem II was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>Loll, B., Kern, J., Saenger, W., Zouni, A., Biesiadka, J. "Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II." Nature 2005, 438: 1040-1044. PMID: [http://www.ncbi.nlm.nih.gov/pubmed/16355230 16355230]</ref> and at 3.50 Å <ref>Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J., Iwata, S. "Architecture of the photosynthetic oxygen-evolving center." Science, March 19, 2004, 303 (5665), 1831-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14764885 14764885]</ref>. PDB codes are [http://www.proteopedia.org/wiki/index.php/2AXT 2AXT] and [http://www.proteopedia.org/wiki/index.php/1S5L 1S5L], respectively. Cyanobacteria and plants both contain Photosystem II while photosynthetic bacteria contain the bacterial reaction center. This photosynthetic protein complex is associated with a variety of functional ligands. It is a <scene name='Photosystem_II/Psii_dimer/1'>dimer</scene> composed mainly of alpha-helices. Nineteen <scene name='Photosystem_II/Protein_only/1'>subunits</scene> are in each monomer, with multiple extrinsic subunits associated with the oxygen evolving complex missing from this crystallization. Photosystem II is a membrane bound protein complex that in plants is associated with the thylakoid membrane of chloroplasts. <scene name='Photosystem_II/Hydrophobic_polar/1'>Polar and hydrophobic</scene> regions correlate with membrane associated nature of the protein. '''<FONT COLOR="#616D7E">Hydrophobic</FONT>''' helices make up the transmembranal portion, while '''<FONT COLOR="#C031C7">polar</FONT>''' residues are concentrated externally on either side of the membrane. | ||
==Photosynthesis== | ==Photosynthesis== |