User:Clara Costa D'Elia/Sandbox 1

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Each individual light-harvesting complex is composed of oligomers of short peptides (α and β) with associated pigments (Hawthornthwaite & Cogdell, 1991). αβ apoproteins with their non-covalently bound carotenoid and bacteriochlorophyll (Bchl ) pigments form the multi-subunit complexes LH1 and LH2
Each individual light-harvesting complex is composed of oligomers of short peptides (α and β) with associated pigments (Hawthornthwaite & Cogdell, 1991). αβ apoproteins with their non-covalently bound carotenoid and bacteriochlorophyll (Bchl ) pigments form the multi-subunit complexes LH1 and LH2
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== Secondary Structure ==
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== Structure ==
The differences between the LH1 and LH2 complexes reside in their protein/pigment stoichiometry and modes of oligomerization. Structural studies have shown that LH2 complexes are formed from eight or nine αβ subunit oligomers
The differences between the LH1 and LH2 complexes reside in their protein/pigment stoichiometry and modes of oligomerization. Structural studies have shown that LH2 complexes are formed from eight or nine αβ subunit oligomers
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Each apoprotein possesses a long trans-membrane α-helix.
 
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In the β apoprotein the trans-membrane (8-9 turn) helix begins after a four-residue N-terminal extended section.
 
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The β apoprotein trans-membrane helix is slightly curved and is inclined to the C9 axis at an angle of approximately 15°. The membrane-spanning segment of the α apoprotein is, in the main, parallel with the C9 axis.
 
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== Tertiary structure ==
 
Structural studies have shown that LH2 complexes are formed from nine ab <scene name='91/911263/Alpha_carbon_lhc_ba_ii/1'>Alpha Beta subunits</scene>, organised in a ring of inner a and outer b-peptides. In between the b-peptides and close to the cytoplasmic surface, aswell as Near the
Structural studies have shown that LH2 complexes are formed from nine ab <scene name='91/911263/Alpha_carbon_lhc_ba_ii/1'>Alpha Beta subunits</scene>, organised in a ring of inner a and outer b-peptides. In between the b-peptides and close to the cytoplasmic surface, aswell as Near the
periplasmic surface, and between a and b- peptides, are <scene name='91/911263/Bacteriochlorophylls/1'>Bacteriochlorophylls</scene>, they are responsible for near infrared absorption, being called B800 and B850.
periplasmic surface, and between a and b- peptides, are <scene name='91/911263/Bacteriochlorophylls/1'>Bacteriochlorophylls</scene>, they are responsible for near infrared absorption, being called B800 and B850.
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<scene name='91/911263/Rhodopin_glucoside/1'> Carotenoids</scene>pigments are also present and absorb in the visible part of the spectrum and perform the additional role of protection against photo-induced oxidation
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<scene name='91/911263/Rhodopin_glucoside/1'> Carotenoids</scene>pigments are also present and absorb in the visible part of the spectrum and perform the additional role of protection against photo-induced oxidation, in the case of the LHC II the carotenoid present is rhodopin glucoside.
<scene name='91/911263/Water_molecules_on_the_lhc_ii/1'>Water molecules</scene>
<scene name='91/911263/Water_molecules_on_the_lhc_ii/1'>Water molecules</scene>
<scene name='91/911263/Side_chains_of_the_lhc_ii/1'>Side chains</scene>
<scene name='91/911263/Side_chains_of_the_lhc_ii/1'>Side chains</scene>
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== Relevance ==
== Relevance ==

Revision as of 18:44, 31 May 2022

Light Harvesting Complex II

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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Clara Costa D'Elia

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