2bhw: Difference between revisions

Latest revision as of 09:03, 16 September 2026

PEA LIGHT-HARVESTING COMPLEX II AT 2.5 ANGSTROM RESOLUTION

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.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	CLA, DGD, LHG, LUX, NEX, XAT
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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

[1]

[2]

[3]

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[2bhw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHW FirstGlance]. <br>
 </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHL:CHLOROPHYLL+B'>CHL</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LUX:(3R,3R,6S,9R,9R,13R,13S)-4,5-DIDEHYDRO-5,6,7,8,9,9,10,10,11,11,12,12,13,13,14,14,15,15-OCTADECAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>LUX</scene>, <scene name='pdbligand=NEX:(1R,3R)-6-{(3E,5E,7E,9E,11E,13E,15E,17E)-18-[(1S,4R,6R)-4-HYDROXY-2,2,6-TRIMETHYL-7-OXABICYCLO[4.1.0]HEPT-1-YL]-3,7,12,16-TETRAMETHYLOCTADECA-1,3,5,7,9,11,13,15,17-NONAENYLIDENE}-1,5,5-TRIMETHYLCYCLOHEXANE-1,3-DIOL'>NEX</scene>, <scene name='pdbligand=XAT:(3S,5R,6S,3S,5R,6S)-5,6,5,6-DIEPOXY-5,6,5,6-+TETRAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>XAT</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LUX:(3R,3R,6S,9R,9R,13R,13S)-4,5-DIDEHYDRO-5,6,7,8,9,9,10,10,11,11,12,12,13,13,14,14,15,15-OCTADECAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>LUX</scene>, <scene name='pdbligand=NEX:(1R,3S)-6-[(5E,7E,9E,11E,13E,15Z,17E)-18-[(1R,3S,6S)-3-hydroxy-1,5,5-trimethyl-7-oxabicyclo[4.1.0]heptan-6-yl]-3,7,12,16-tetramethyl-octadeca-1,3,5,7,9,11,13,15,17-nonaenylidene]-1,5,5-trimethyl-cyclohexane-1,3-diol'>NEX</scene>, <scene name='pdbligand=XAT:(3S,5R,6S,3S,5R,6S)-5,6,5,6-DIEPOXY-5,6,5,6-+TETRAHYDRO-BETA,BETA-CAROTENE-3,3-DIOL'>XAT</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhw OCA], [https://pdbe.org/2bhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhw RCSB], [https://www.ebi.ac.uk/pdbsum/2bhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhw ProSAT]</span></td></tr>
 </table>
@@ Line 15: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bhw_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bhw ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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<ref>PMID:15719016</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bhw" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2bhw: Difference between revisions

Latest revision as of 09:03, 16 September 2026

PEA LIGHT-HARVESTING COMPLEX II AT 2.5 ANGSTROM RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

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