2x5u: Difference between revisions
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==80 microsecond Laue diffraction snapshot from crystals of a photosynthetic reaction centre without illumination.== | |||
<StructureSection load='2x5u' size='340' side='right'caption='[[2x5u]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x5u]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X5U FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</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=2x5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x5u OCA], [https://pdbe.org/2x5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x5u RCSB], [https://www.ebi.ac.uk/pdbsum/2x5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x5u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CYCR_BLAVI CYCR_BLAVI] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.<ref>PMID:10736158</ref> | |||
== 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/x5/2x5u_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2x5u ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Photosynthetic reaction centers convert the energy content of light into a transmembrane potential difference and so provide the major pathway for energy input into the biosphere. We applied time-resolved Laue diffraction to study light-induced conformational changes in the photosynthetic reaction center complex of Blastochloris viridis. The side chain of TyrL162, which lies adjacent to the special pair of bacteriochlorophyll molecules that are photooxidized in the primary light conversion event of photosynthesis, was observed to move 1.3 angstroms closer to the special pair after photoactivation. Free energy calculations suggest that this movement results from the deprotonation of this conserved tyrosine residue and provides a mechanism for stabilizing the primary charge separation reactions of photosynthesis. | |||
Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction.,Wohri AB, Katona G, Johansson LC, Fritz E, Malmerberg E, Andersson M, Vincent J, Eklund M, Cammarata M, Wulff M, Davidsson J, Groenhof G, Neutze R Science. 2010 Apr 30;328(5978):630-3. PMID:20431017<ref>PMID:20431017</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x5u" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Cytochrome | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Blastochloris viridis]] | [[Category: Blastochloris viridis]] | ||
[[Category: Andersson | [[Category: Large Structures]] | ||
[[Category: Cammarata | [[Category: Andersson M]] | ||
[[Category: Davidsson | [[Category: Cammarata M]] | ||
[[Category: Eklund | [[Category: Davidsson J]] | ||
[[Category: Fritz | [[Category: Eklund M]] | ||
[[Category: Groenhof | [[Category: Fritz E]] | ||
[[Category: Johansson | [[Category: Groenhof G]] | ||
[[Category: Katona | [[Category: Johansson LC]] | ||
[[Category: Malmerberg | [[Category: Katona G]] | ||
[[Category: Neutze | [[Category: Malmerberg E]] | ||
[[Category: Vincent | [[Category: Neutze R]] | ||
[[Category: Wohri | [[Category: Vincent J]] | ||
[[Category: Wulff | [[Category: Wohri AB]] | ||
[[Category: Wulff M]] | |||
Latest revision as of 13:24, 20 December 2023
80 microsecond Laue diffraction snapshot from crystals of a photosynthetic reaction centre without illumination.80 microsecond Laue diffraction snapshot from crystals of a photosynthetic reaction centre without illumination.
Structural highlights
FunctionCYCR_BLAVI The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[1] 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 PubMedPhotosynthetic reaction centers convert the energy content of light into a transmembrane potential difference and so provide the major pathway for energy input into the biosphere. We applied time-resolved Laue diffraction to study light-induced conformational changes in the photosynthetic reaction center complex of Blastochloris viridis. The side chain of TyrL162, which lies adjacent to the special pair of bacteriochlorophyll molecules that are photooxidized in the primary light conversion event of photosynthesis, was observed to move 1.3 angstroms closer to the special pair after photoactivation. Free energy calculations suggest that this movement results from the deprotonation of this conserved tyrosine residue and provides a mechanism for stabilizing the primary charge separation reactions of photosynthesis. Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction.,Wohri AB, Katona G, Johansson LC, Fritz E, Malmerberg E, Andersson M, Vincent J, Eklund M, Cammarata M, Wulff M, Davidsson J, Groenhof G, Neutze R Science. 2010 Apr 30;328(5978):630-3. PMID:20431017[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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