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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1ijd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJD FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1ijd]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IJD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=RPA:RHODOPINAL+GLUCOSIDE'>RPA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=RPA:RHODOPINAL+GLUCOSIDE'>RPA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kzu|1kzu]], [[1lgh|1lgh]]</div></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=1ijd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ijd OCA], [https://pdbe.org/1ijd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ijd RCSB], [https://www.ebi.ac.uk/pdbsum/1ijd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ijd ProSAT]</span></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=1ijd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ijd OCA], [https://pdbe.org/1ijd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ijd RCSB], [https://www.ebi.ac.uk/pdbsum/1ijd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ijd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LHA1_RHOAC LHA1_RHOAC]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. [[https://www.uniprot.org/uniprot/LHB1_RHOAC LHB1_RHOAC]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
| + | [https://www.uniprot.org/uniprot/LHB1_RHOAC LHB1_RHOAC] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Rhodoblastus acidophilus]] | | [[Category: Rhodoblastus acidophilus]] |
| - | [[Category: Cogdell, R J]] | + | [[Category: Cogdell RJ]] |
| - | [[Category: Isaacs, N W]] | + | [[Category: Isaacs NW]] |
| - | [[Category: McLuskey, K]] | + | [[Category: McLuskey K]] |
| - | [[Category: Prince, S M]] | + | [[Category: Prince SM]] |
| - | [[Category: Alpha-helix apoprotein]]
| + | |
| - | [[Category: Intergral membrane protein]]
| + | |
| - | [[Category: Light harvesting]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Pigment-protein complex]]
| + | |
| Structural highlights
Function
LHB1_RHOAC Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
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 B800-820, or LH3, complex is a spectroscopic variant of the B800-850 LH2 peripheral light-harvesting complex. LH3 is synthesized by some species and strains of purple bacteria when growing under what are generally classed as "stressed" conditions, such as low intensity illumination and/or low temperature (<30 degrees C). The apoproteins in these complexes modify the absorption properties of the chromophores to ensure that the photosynthetic process is highly efficient. The crystal structure of the B800-820 light-harvesting complex, an integral membrane pigment-protein complex, from the purple bacteria Rhodopseudomonas (Rps.) acidophila strain 7050 has been determined to a resolution of 3.0 A by molecular replacement. The overall structure of the LH3 complex is analogous to that of the LH2 complex from Rps. acidophila strain 10050. LH3 has a nonameric quaternary structure where two concentric cylinders of alpha-helices enclose the pigment molecules bacteriochlorophyll a and carotenoid. The observed spectroscopic differences between LH2 and LH3 can be attributed to differences in the primary structure of the apoproteins. There are changes in hydrogen bonding patterns between the coupled Bchla molecules and the protein that have an effect on the conformation of the C3-acetyl groups of the B820 molecules. The structure of LH3 shows the important role that the protein plays in modulating the characteristics of the light-harvesting system and indicates the mechanisms by which the absorption properties of the complex are altered to produce a more efficient light-harvesting component.
The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050.,McLuskey K, Prince SM, Cogdell RJ, Isaacs NW Biochemistry. 2001 Jul 31;40(30):8783-9. PMID:11467938[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McLuskey K, Prince SM, Cogdell RJ, Isaacs NW. The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050. Biochemistry. 2001 Jul 31;40(30):8783-9. PMID:11467938
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