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| - | [[Image:2jj0.jpg|left|200px]] | |
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| - | {{Structure
| + | ==PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M248 REPLACED WITH TRP (CHAIN M, AM248W)== |
| - | |PDB= 2jj0 |SIZE=350|CAPTION= <scene name='initialview01'>2jj0</scene>, resolution 2.80Å
| + | <StructureSection load='2jj0' size='340' side='right'caption='[[2jj0]], [[Resolution|resolution]] 2.80Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene> and <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene> | + | <table><tr><td colspan='2'>[[2jj0]] 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=2JJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JJ0 FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | |GENE=
| + | <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=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</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'>[https://proteopedia.org/fgij/fg.htm?mol=2jj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jj0 OCA], [https://pdbe.org/2jj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jj0 RCSB], [https://www.ebi.ac.uk/pdbsum/2jj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jj0 ProSAT]</span></td></tr> |
| - | | + | </table> |
| - | '''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M248 REPLACED WITH TRP (CHAIN M, AM248W)''' | + | == Function == |
| - | | + | [https://www.uniprot.org/uniprot/RCEH_CERSP RCEH_CERSP] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. |
| - | | + | == Evolutionary Conservation == |
| - | ==Overview== | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | X-ray crystallography has been used to investigate the extent of structural changes in mutants of the purple bacterial reaction center that assemble without a particular ubiquinone or bacteriopheophytin cofactor. In the case of the bacteriopheophytin-exclusion mutant, in which Ala M149 was replaced by Trp (AM149W), the quality of protein crystals was improved over that seen in previous work by minimizing illumination, time, and temperature during the purification protocol and carrying out crystal growth at 4 degrees C after overnight incubation at 18 degrees C. The X-ray crystal structure of the AM149W mutant, determined to a resolution of 2.2 A, showed very little change in protein structure despite the absence of the bacteriopheophytin cofactor. Changes in the electron density map in the region of the cofactor binding site could be accounted for by changes in the conformation of the phytol side chains of adjacent cofactors and the presence of a buried water molecule. Residues lining the vacated binding pocket did not show any significant changes in conformation or increases in disorder as assessed through crystallographic atomic displacement parameters (B-factors). The X-ray crystal structure of a reaction center lacking the primary acceptor ubiquinone through mutation of Ala M248 to Trp (AM248W) was also determined, to a resolution of 2.8 A. Again, despite the absence of an internal cofactor only very minor changes in protein structure were observed. This is in contrast to a previous report on a reaction center lacking this ubiquinone through mutation of Ala M260 to Trp (AM260W) where more extensive changes in structure were apparent. All three mutant reaction centers showed a decrease in thermal stability when housed in the native membrane, but this decrease was smaller for the AM260W mutant than the AM248W complex, possibly due to beneficial effects of the observed changes in protein structure. The lack of major changes in protein structure despite the absence of large internal cofactors is discussed in terms of protein rigidity, the protective influence of the adaptable membrane environment, and the role of small molecules and ions as packing material in the internal cavities created by this type of mutation.
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==About this Structure==
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/2jj0_consurf.spt"</scriptWhenChecked> |
| - | 2JJ0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJ0 OCA].
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==Reference==
| + | </jmolCheckbox> |
| - | Structural responses to cavity-creating mutations in an integral membrane protein., Fyfe PK, Potter JA, Cheng J, Williams CM, Watson AJ, Jones MR, Biochemistry. 2007 Sep 18;46(37):10461-72. Epub 2007 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17711306 17711306]
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jj0 ConSurf]. |
| - | [[Category: Protein complex]] | + | <div style="clear:both"></div> |
| - | [[Category: Rhodobacter sphaeroides]]
| + | __TOC__ |
| - | [[Category: Cheng, J.]]
| + | </StructureSection> |
| - | [[Category: Fyfe, P K.]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Jones, M R.]]
| + | [[Category: Large Structures]] |
| - | [[Category: Potter, J.]]
| + | [[Category: Cheng J]] |
| - | [[Category: Watson, A J.]]
| + | [[Category: Fyfe PK]] |
| - | [[Category: Williams, C.]] | + | [[Category: Jones MR]] |
| - | [[Category: BCL]]
| + | [[Category: Potter JA]] |
| - | [[Category: BPH]]
| + | [[Category: Watson AJ]] |
| - | [[Category: CDL]]
| + | [[Category: Williams CM]] |
| - | [[Category: CL]]
| + | |
| - | [[Category: FE]]
| + | |
| - | [[Category: SPN]]
| + | |
| - | [[Category: U10]] | + | |
| - | [[Category: bacteriochlorophyll]] | + | |
| - | [[Category: chlorophyll]] | + | |
| - | [[Category: chromophore]]
| + | |
| - | [[Category: electron transport]]
| + | |
| - | [[Category: iron]]
| + | |
| - | [[Category: magnesium]] | + | |
| - | [[Category: membrane]] | + | |
| - | [[Category: membrane protein]] | + | |
| - | [[Category: metal-binding]] | + | |
| - | [[Category: photosynthesis]] | + | |
| - | [[Category: photosynthetic reaction center]] | + | |
| - | [[Category: reaction center]] | + | |
| - | [[Category: transmembrane]] | + | |
| - | [[Category: transport]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:35 2008''
| + | |
