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| | ==Photosynthetic Reaction Center Mutant With Thr M 21 Replaced With Asp== | | ==Photosynthetic Reaction Center Mutant With Thr M 21 Replaced With Asp== |
| - | <StructureSection load='1jgx' size='340' side='right' caption='[[1jgx]], [[Resolution|resolution]] 3.01Å' scene=''> | + | <StructureSection load='1jgx' size='340' side='right'caption='[[1jgx]], [[Resolution|resolution]] 3.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jgx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JGX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jgx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JGX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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]] 3.01Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jgw|1jgw]], [[1jgy|1jgy]], [[1jgz|1jgz]], [[1jh0|1jh0]]</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=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></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=1jgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgx OCA], [http://pdbe.org/1jgx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jgx RCSB], [http://www.ebi.ac.uk/pdbsum/1jgx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jgx 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=1jgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgx OCA], [https://pdbe.org/1jgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jgx RCSB], [https://www.ebi.ac.uk/pdbsum/1jgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jgx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RCEL_RHOSH RCEL_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEH_RHOSH RCEH_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEM_RHOSH RCEM_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | + | [https://www.uniprot.org/uniprot/RCEL_CERSP RCEL_CERSP] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Allen, J P]] | + | [[Category: Large Structures]] |
| - | [[Category: Camara-Artigas, A]] | + | [[Category: Allen JP]] |
| - | [[Category: Magee, C L]] | + | [[Category: Camara-Artigas A]] |
| - | [[Category: Williams, J C]] | + | [[Category: Magee CL]] |
| - | [[Category: Alpha helix]]
| + | [[Category: Williams JC]] |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
1jgx is a 3 chain structure with sequence from Cereibacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 3.01Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RCEL_CERSP The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
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 role of contact interactions in the crystallization of membrane proteins was assessed by mutation of amino-acid residues on the surface of the reaction center from Rhodobacter sphaeroides. Five single-site mutants were constructed, with changes in contact regions found in the trigonal and tetragonal forms but not the orthorhombic form. Crystallization trials for the tetragonal form yielded either no crystals or crystals with an altered morphology, whereas crystals grew in the other two forms, indicating that these interactions are essential for the stability of the tetragonal crystals. Changes in the structures determined by X-ray diffraction of trigonal crystals for each mutant were related to the quality of the diffraction. Significant differences in the resolution limit of the crystals were associated with the loss of specific interactions between neighboring proteins. The results suggest that the contact regions are crucial for obtaining highly ordered crystals of membrane proteins.
Individual interactions influence the crystalline order for membrane proteins.,Camara-Artigas A, Magee CL, Williams JC, Allen JP Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1281-6. Epub 2001, Aug 23. PMID:11526320[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Camara-Artigas A, Magee CL, Williams JC, Allen JP. Individual interactions influence the crystalline order for membrane proteins. Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1281-6. Epub 2001, Aug 23. PMID:11526320
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