2jj0: Difference between revisions

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{{Seed}}
[[Image:2jj0.png|left|200px]]


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==PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M248 REPLACED WITH TRP (CHAIN M, AM248W)==
The line below this paragraph, containing "STRUCTURE_2jj0", creates the "Structure Box" on the page.
<StructureSection load='2jj0' size='340' side='right'caption='[[2jj0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
{{STRUCTURE_2jj0|  PDB=2jj0  |  SCENE=  }}
<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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/2jj0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M248 REPLACED WITH TRP (CHAIN M, AM248W)===
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:17711306<ref>PMID:17711306</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 17711306 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17711306}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Cereibacter sphaeroides]]
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].
[[Category: Large Structures]]
 
[[Category: Cheng J]]
==Reference==
[[Category: Fyfe PK]]
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]
[[Category: Jones MR]]
 
[[Category: Potter JA]]
On the role of basic residues in adapting the reaction centre-LH1 complex for growth at elevated temperatures in purple bacteria., Watson AJ, Hughes AV, Fyfe PK, Wakeham MC, Holden-Dye K, Heathcote P, Jones MR, Photosynth Res. 2005 Nov;86(1-2):81-100. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16172928 16172928]
[[Category: Watson AJ]]
 
[[Category: Williams CM]]
Structural details of an interaction between cardiolipin and an integral membrane protein., McAuley KE, Fyfe PK, Ridge JP, Isaacs NW, Cogdell RJ, Jones MR, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14706-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10611277 10611277]
 
Ubiquinone binding, ubiquinone exclusion, and detailed cofactor conformation in a mutant bacterial reaction center., McAuley KE, Fyfe PK, Ridge JP, Cogdell RJ, Isaacs NW, Jones MR, Biochemistry. 2000 Dec 12;39(49):15032-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106481 11106481]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Cheng, J.]]
[[Category: Fyfe, P K.]]
[[Category: Jones, M R.]]
[[Category: Potter, J.]]
[[Category: Watson, A J.]]
[[Category: Williams, C.]]
[[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]]
 
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