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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2fkw]] is a 18 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=2FKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKW FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2fkw]] is a 18 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=2FKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKW 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=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=RG1:RHODOPIN+B-D-GLUCOSIDE'>RG1</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]] 2.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</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=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=RG1:RHODOPIN+B-D-GLUCOSIDE'>RG1</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;'>[[1nzu|1nzu]], [[1nkz|1nkz]]</div></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkw OCA], [https://pdbe.org/2fkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkw RCSB], [https://www.ebi.ac.uk/pdbsum/2fkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkw 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=2fkw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkw OCA], [https://pdbe.org/2fkw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkw RCSB], [https://www.ebi.ac.uk/pdbsum/2fkw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkw ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/LHA4_RHOAC LHA4_RHOAC]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. [[https://www.uniprot.org/uniprot/LHB5_RHOAC LHB5_RHOAC]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
| + | [https://www.uniprot.org/uniprot/LHA4_RHOAC LHA4_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: Caffrey, M]] | + | [[Category: Caffrey M]] |
| - | [[Category: Cherezov, V]] | + | [[Category: Cherezov V]] |
| - | [[Category: Clogston, J]] | + | [[Category: Clogston J]] |
| - | [[Category: Papiz, M Z]] | + | [[Category: Papiz MZ]] |
| - | [[Category: Crystallization]]
| + | |
| - | [[Category: Cubic phase]]
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| - | [[Category: Ldao]]
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| - | [[Category: Light harvesting complex b800-b850]]
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| - | [[Category: Lipidic mesophase]]
| + | |
| - | [[Category: Membrane protein]]
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| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Rhodopin glucoside carotenoid]]
| + | |
| - | [[Category: Sponge phase]]
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| Structural highlights
Function
LHA4_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 cubic phase or in meso crystallization method is responsible for almost 40 solved integral membrane protein structures. Most of these are small and compact proteins. A model for how crystals form by the in meso method has been proposed that invokes a transition between mesophases. In light of this model, we speculated that a more hydrated and open mesophase, of reduced interfacial curvature, would support facile crystallization of bigger and bulkier proteins. The proposal was explored here by performing crystallization in the presence of additives that swell the cubic phase. The additive concentration inducing swelling, as quantified by small-angle X-ray diffraction, coincided with a "crystallization window" in which two, very different transmembranal proteins produced crystals. That the swollen mesophase can grow structure-grade crystals was proven with one of these, the light-harvesting II complex. In most regards, the structural details of the corresponding complex resembled those of crystals grown by the conventional vapour diffusion method, with some important differences. In particular, packing density in the in meso-grown crystals was dramatically higher, more akin to that seen with water-soluble proteins, which accounts for their enhanced diffracting power. The layered and close in-plane packing observed has been rationalized in a model for nucleation and crystal growth by the in meso method that involves swollen mesophases. These results present a rational case for including mesophase-swelling additives in screens for in meso crystallogenesis. Their use will contribute to broadening the range of membrane proteins that yield to structure determination.
Room to move: crystallizing membrane proteins in swollen lipidic mesophases.,Cherezov V, Clogston J, Papiz MZ, Caffrey M J Mol Biol. 2006 Apr 14;357(5):1605-18. Epub 2006 Feb 2. PMID:16490208[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cherezov V, Clogston J, Papiz MZ, Caffrey M. Room to move: crystallizing membrane proteins in swollen lipidic mesophases. J Mol Biol. 2006 Apr 14;357(5):1605-18. Epub 2006 Feb 2. PMID:16490208 doi:10.1016/j.jmb.2006.01.049
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