Photosystem II: Difference between revisions
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<applet load="1s5l" size="500" frame="true" align="right" /> | <applet load="1s5l" size="500" frame="true" align="right" /> | ||
[[Image:1s5l.gif| | [[Image:1s5l.gif|250px|left]] | ||
==Background== | ==Background== | ||
This structure of Photosystem II was crystallized from the bacteria, ''Thermosynechococcus elongatus'', at 3.50 Å. Cyanobacteria and plants both contain Photosystem II with a similar structure. This photosynthetic protein 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 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 bacteria, ''Thermosynechococcus elongatus'', at 3.50 Å. Cyanobacteria and plants both contain Photosystem II with a similar structure. This photosynthetic protein 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 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. | ||
