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| | <StructureSection load='1nkz' size='340' side='right'caption='[[1nkz]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1nkz' size='340' side='right'caption='[[1nkz]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nkz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25092 Atcc 25092] and [http://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NKZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nkz]] 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=1NKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NKZ 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=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</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]] 2Å</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=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</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">[[1kzu|1kzu]]</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=1nkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nkz OCA], [https://pdbe.org/1nkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nkz RCSB], [https://www.ebi.ac.uk/pdbsum/1nkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nkz ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nkz OCA], [http://pdbe.org/1nkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nkz RCSB], [http://www.ebi.ac.uk/pdbsum/1nkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nkz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LHA4_RHOAC LHA4_RHOAC]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. [[http://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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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nk/1nkz_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nk/1nkz_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> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 25092]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Rhodoblastus acidophilus]] | | [[Category: Rhodoblastus acidophilus]] |
| - | [[Category: Cogdell, R J]] | + | [[Category: Cogdell RJ]] |
| - | [[Category: Howard, T]] | + | [[Category: Howard T]] |
| - | [[Category: Isaacs, N W]] | + | [[Category: Isaacs NW]] |
| - | [[Category: Papiz, M Z]] | + | [[Category: Papiz MZ]] |
| - | [[Category: Prince, S M]] | + | [[Category: Prince SM]] |
| - | [[Category: Bacteriochlorophyll some]]
| + | |
| - | [[Category: Light harvesting complex ii]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Rhodopin glucoside]]
| + | |
| - | [[Category: Trans-membrane helice]]
| + | |
| 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 structure at 100K of integral membrane light-harvesting complex II (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to 2.0A resolution. The electron density has been significantly improved, compared to the 2.5A resolution map, by high resolution data, cryo-cooling and translation, libration, screw (TLS) refinement. The electron density reveals a second carotenoid molecule, the last five C-terminal residues of the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand of the B800 bacteriochlorophyll. TLS refinement has enabled the characterisation of displacements between molecules in the complex. B850 bacteriochlorophyll molecules are arranged in a ring of 18 pigments composed of nine approximate dimers. These pigments are strongly coupled and at their equilibrium positions the excited state dipole interaction energies, within and between dimers, are approximately 370cm(-1) and 280cm(-1), respectively. This difference in coupling energy is similar in magnitude to changes in interaction energies arising from the pigment displacements described by TLS tensors. The displacements appear to be non-random in nature and appear to be designed to optimise the modulation of pigment energy interactions. This is the first time that LH2 pigment displacements have been quantified experimentally. The calculated energy changes indicate that there may be significant contributions to inter-pigment energy interactions from molecular displacements and these may be of importance to photosynthetic energy transfer.
The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions.,Papiz MZ, Prince SM, Howard T, Cogdell RJ, Isaacs NW J Mol Biol. 2003 Mar 7;326(5):1523-38. PMID:12595263[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Papiz MZ, Prince SM, Howard T, Cogdell RJ, Isaacs NW. The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions. J Mol Biol. 2003 Mar 7;326(5):1523-38. PMID:12595263
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