Photosystem II
From Proteopedia
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<StructureSection load='3a0b' size='400' caption='Photosystem II, [[3a0b]]' scene='' > | <StructureSection load='3a0b' size='400' caption='Photosystem II, [[3a0b]]' scene='' > | ||
- | [[Image:1s5l.gif|250px|left]] | ||
==Background== | ==Background== | ||
This structure of '''Photosystem II''' was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>PMID: 16355230</ref> and at 3.50 Å <ref>PMID: 14764885</ref>. PDB codes are [[2axt]] and [[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. | This structure of '''Photosystem II''' was crystallized from the cyanobacteria, ''Thermosynechococcus elongatus'', at 3.0Å <ref>PMID: 16355230</ref> and at 3.50 Å <ref>PMID: 14764885</ref>. PDB codes are [[2axt]] and [[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. |
Revision as of 06:45, 20 August 2014
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3D structures of photosystem II
Updated on 20-August-2014
3arc, 3a0b, 3a0h, 4il6 – PSII – Thermosynechococcus vulcanos
3prq, 3prr - TePSII + terbutryn – Thermosynechococcus elongatus
3kzi, 3bz1, 3bz2, 2axt, 1w5c, 1s5l, 1izl, 1ilx, 1fe1, 4fby, 4ixr, 4ixq – TePSII
3zpn - TePSII PSB28 protein
4k7b - PSII extrinsic protein – Chaetoceros gracilis
2y6x – TePSII PSB27 protein
2kvo – SyPSII reaction center PSB28 protein – Synechocystis – NMR
2kmf, 2knd - SyPSII reaction center PSB27 subunit – NMR
2vu4, 1vyk – spPSII PSBP subunit – spinach
1nze - spPSII PSBQ subunit
1v2b - PSII PSBP subunit – tobacco
1fc6, 1fc7, 1fc9, 1fcf – PSII C terminal processing protease – Scenedesmus obliquus
Additional Resources
For additional information, see: Photosynthesis
References
- ↑ 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 Dec 15;438(7070):1040-4. PMID:16355230 doi:http://dx.doi.org/10.1038/nature04224
- ↑ Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S. Architecture of the photosynthetic oxygen-evolving center. Science. 2004 Mar 19;303(5665):1831-8. Epub 2004 Feb 5. PMID:14764885 doi:http://dx.doi.org/10.1126/science.1093087
- ↑ Ferreira KN, Iverson TM, Maghlaoui K, Barber J, Iwata S. Architecture of the photosynthetic oxygen-evolving center. Science. 2004 Mar 19;303(5665):1831-8. Epub 2004 Feb 5. PMID:14764885 doi:http://dx.doi.org/10.1126/science.1093087
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