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| - | ==LIGHT-HARVESTING COMPLEX 1 BETA SUBUNIT FROM RHODOBACTER SPHAEROIDES== | + | |
| - | <StructureSection load='1dx7' size='340' side='right' caption='[[1dx7]], [[NMR_Ensembles_of_Models | 6 NMR models]]' scene=''> | + | ==Light-harvesting complex 1 beta subunit from Rhodobacter sphaeroides== |
| | + | <StructureSection load='1dx7' size='340' side='right'caption='[[1dx7]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dx7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DX7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dx7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DX7 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx7 OCA], [http://pdbe.org/1dx7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1dx7 PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1dx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx7 OCA], [https://pdbe.org/1dx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dx7 RCSB], [https://www.ebi.ac.uk/pdbsum/1dx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dx7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LHB1_RHOSH LHB1_RHOSH]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. | + | [https://www.uniprot.org/uniprot/LHB1_CERSP LHB1_CERSP] 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]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/1dx7_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/1dx7_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Conroy, M J]] | + | [[Category: Large Structures]] |
| - | [[Category: Hunter, C N]] | + | [[Category: Conroy MJ]] |
| - | [[Category: Loach, P A]] | + | [[Category: Hunter CN]] |
| - | [[Category: Parkes-Loach, P S]] | + | [[Category: Loach PA]] |
| - | [[Category: Westerhuis, W]] | + | [[Category: Parkes-Loach PS]] |
| - | [[Category: Williamson, M P]] | + | [[Category: Westerhuis W]] |
| - | [[Category: Bacteriochlorophyll binding]]
| + | [[Category: Williamson MP]] |
| - | [[Category: Light harvesting]]
| + | |
| - | [[Category: Light-harvesting protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Photosynthesis]]
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| Structural highlights
Function
LHB1_CERSP 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
Here, the solution structure of the Rhodobacter sphaeroides core light-harvesting complex beta polypeptide solubilised in chloroform:methanol is presented. The structure, determined by homonuclear NMR spectroscopy and distance geometry, comprises two alpha helical regions (residue -34 to -15 and -11 to +6, using the numbering system in which the conserved histidine residue is numbered zero) joined by a more flexible four amino acid residue linker. The C-terminal helix forms the membrane spanning region in the intact LH1 complex, whilst the N-terminal helix must lie in the lipid head groups or in the cytoplasm, and form the basis of interaction with the alpha polypeptide. The structure of a mutant beta polypeptide W(+9)F was also determined. This mutant, which is deficient in a hydrogen bond donor to the bacteriochlorophyll, showed an identical structure to the wild-type, implying that observed differences in interaction with other LH1 polypeptides must arise from cofactor binding. Using these structures we propose a modification to existing models of the intact LH1 complex by replacing the continuous helix of the beta polypeptide with two helices, one of which lies at an acute angle to the membrane plane. We suggest that a key difference between LH1 and LH2 is that the beta subunit is more bent in LH1. This modification puts the N terminus of LH1beta close to the reaction centre H subunit, and provides a rationale for the different ring sizes of LH1 and LH2 complexes.
The solution structure of Rhodobacter sphaeroides LH1beta reveals two helical domains separated by a more flexible region: structural consequences for the LH1 complex.,Conroy MJ, Westerhuis WH, Parkes-Loach PS, Loach PA, Hunter CN, Williamson MP J Mol Biol. 2000 Apr 21;298(1):83-94. PMID:10756106[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Conroy MJ, Westerhuis WH, Parkes-Loach PS, Loach PA, Hunter CN, Williamson MP. The solution structure of Rhodobacter sphaeroides LH1beta reveals two helical domains separated by a more flexible region: structural consequences for the LH1 complex. J Mol Biol. 2000 Apr 21;298(1):83-94. PMID:10756106 doi:10.1006/jmbi.2000.3649
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