User:R. Jeremy Johnson/Sandbox 1: Difference between revisions

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==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, Dec 15, 2005, 438(7070), 1040-4.  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 [[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>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, Dec 15, 2005, 438(7070), 1040-4.  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 [[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.
<ref>DOI: 10.1038/s41586-022-04845-4 </ref>
<Ref> Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, Ohto U. Structure of the bile acid transporter and HBV receptor NTCP. Nature. 2022 Jun;606(7916):1021-1026. [https://dx.doi.org/10.1038/s41586-022-04845-4 DOI: 10.1038/s41586-022-04845-4]. </Ref>


==Basic Structure==
==Basic Structure==


<ref name = "Butler"> PMID: 7016210 </ref>
<ref name = "Butler"> PMID: 7016210 </ref>
<scene name='43/436107/Arginine_highlight/4'>Ver4</scene>
<scene name='43/436107/Arginine_highlight/3'>Ver3</scene>
<scene name='43/436107/Arginine_highlight/8'>Ver8</scene>
<scene name='43/436107/Arginine_highlight/7'>Ver7</scene>
<scene name='43/436107/Arginine_highlight/6'>Ver6</scene>
<scene name='43/436107/Arginine_highlight/5'>Ver5</scene>


<scene name='43/436107/Arginine_highlight/2'>Arginine Zoom</scene>
<scene name='43/436107/Arginine_highlight/2'>Arginine Zoom</scene>

Latest revision as of 23:37, 13 March 2023

Ribonuclease A - Structure 7RSA

Drag the structure with the mouse to rotate

[2]

BackgroundBackground

This structure of Photosystem II was crystallized from the cyanobacteria, Thermosynechococcus elongatus, at 3.0Å [1] and at 3.50 Å [2]. 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 composed mainly of alpha-helices. Nineteen 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. regions correlate with membrane associated nature of the protein. Hydrophobic helices make up the transmembranal portion, while polar residues are concentrated externally on either side of the membrane.

[3]

[4]

Basic StructureBasic Structure

[5]

Electron TransferElectron Transfer

[5]

Basic StructureBasic Structure

[6]


Additional ResourcesAdditional Resources


ReferencesReferences

  1. ↑ 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, Dec 15, 2005, 438(7070), 1040-4. PMID:16355230
  2. ↑ 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:14764885
  3. ↑ Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, Ohto U. Structure of the bile acid transporter and HBV receptor NTCP. Nature. 2022 Jun;606(7916):1021-1026. PMID:35580629 doi:10.1038/s41586-022-04845-4
  4. ↑ Asami J, Kimura KT, Fujita-Fujiharu Y, Ishida H, Zhang Z, Nomura Y, Liu K, Uemura T, Sato Y, Ono M, Yamamoto M, Noda T, Shigematsu H, Drew D, Iwata S, Shimizu T, Nomura N, Ohto U. Structure of the bile acid transporter and HBV receptor NTCP. Nature. 2022 Jun;606(7916):1021-1026. DOI: 10.1038/s41586-022-04845-4.
  5. ↑ 5.0 5.1 Banacky P, Linder B. Model of serine proteases charge relay system -- PCILO study. Biophys Chem. 1981 Jun;13(3):223-31. PMID:7016210
  6. ↑ [1]
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