User:Clara Costa D'Elia/Sandbox 1
From Proteopedia
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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 | ||
- | == | + | == 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 | ||
- | Each apoprotein possesses a long trans-membrane α-helix. | ||
- | In the β apoprotein the trans-membrane (8-9 turn) helix begins after a four-residue N-terminal extended section. | ||
- | 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. | ||
- | == 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. | ||
- | <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 | + | <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
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References
- ↑ 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
- ↑ 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