Structural highlights
2bhw is a 3 chain structure with sequence from Pisum sativum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | , , , , , , |
| Related: | 1vcr |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[CB22_PEA] The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.[1] May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The plant light-harvesting complex of photosystem II (LHC-II) collects and transmits solar energy for photosynthesis in chloroplast membranes and has essential roles in regulation of photosynthesis and in photoprotection. The 2.5 A structure of pea LHC-II determined by X-ray crystallography of stacked two-dimensional crystals shows how membranes interact to form chloroplast grana, and reveals the mutual arrangement of 42 chlorophylls a and b, 12 carotenoids and six lipids in the LHC-II trimer. Spectral assignment of individual chlorophylls indicates the flow of energy in the complex and the mechanism of photoprotection in two close chlorophyll a-lutein pairs. We propose a simple mechanism for the xanthophyll-related, slow component of nonphotochemical quenching in LHC-II, by which excess energy is transferred to a zeaxanthin replacing violaxanthin in its binding site, and dissipated as heat. Our structure shows the complex in a quenched state, which may be relevant for the rapid, pH-induced component of nonphotochemical quenching.
Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution.,Standfuss J, Terwisscha van Scheltinga AC, Lamborghini M, Kuhlbrandt W EMBO J. 2005 Mar 9;24(5):919-28. Epub 2005 Feb 17. PMID:15719016[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jahns P, Junge W. Dicyclohexylcarbodiimide-binding proteins related to the short circuit of the proton-pumping activity of photosystem II. Identified as light-harvesting chlorophyll-a/b-binding proteins. Eur J Biochem. 1990 Nov 13;193(3):731-6. PMID:2174365
- ↑ Jahns P, Junge W. Dicyclohexylcarbodiimide-binding proteins related to the short circuit of the proton-pumping activity of photosystem II. Identified as light-harvesting chlorophyll-a/b-binding proteins. Eur J Biochem. 1990 Nov 13;193(3):731-6. PMID:2174365
- ↑ Standfuss J, Terwisscha van Scheltinga AC, Lamborghini M, Kuhlbrandt W. Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution. EMBO J. 2005 Mar 9;24(5):919-28. Epub 2005 Feb 17. PMID:15719016
