1r2c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 30 October 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1r2c.gif|left|200px]]
 
-
{{Structure
+
==PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)==
-
|PDB= 1r2c |SIZE=350|CAPTION= <scene name='initialview01'>1r2c</scene>, resolution 2.86&Aring;
+
<StructureSection load='1r2c' size='340' side='right'caption='[[1r2c]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=BCB:BACTERIOCHLOROPHYLL+B'>BCB</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene>, <scene name='pdbligand=NS5:DIHYDRO-NEUROSPORENE'>NS5</scene> and <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene>
+
<table><tr><td colspan='2'>[[1r2c]] 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=1R2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R2C 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]] 2.86&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=NS5:15-CIS-1,2-DIHYDRONEUROSPORENE'>NS5</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</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=1r2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2c OCA], [https://pdbe.org/1r2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r2c RCSB], [https://www.ebi.ac.uk/pdbsum/1r2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r2c 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/r2/1r2c_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=1r2c ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).
-
'''PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)'''
+
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.,Baxter RH, Ponomarenko N, Srajer V, Pahl R, Moffat K, Norris JR Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5982-7. Epub 2004 Apr 8. PMID:15073325<ref>PMID:15073325</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1r2c" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).
+
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1R2C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R2C OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center., Baxter RH, Ponomarenko N, Srajer V, Pahl R, Moffat K, Norris JR, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5982-7. Epub 2004 Apr 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15073325 15073325]
+
[[Category: Blastochloris viridis]]
[[Category: Blastochloris viridis]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Baxter, R H.]]
+
[[Category: Baxter RH]]
-
[[Category: Moffat, K.]]
+
[[Category: Moffat K]]
-
[[Category: Norris, J R.]]
+
[[Category: Norris JR]]
-
[[Category: Pahl, R.]]
+
[[Category: Pahl R]]
-
[[Category: Ponomarenko, N.]]
+
[[Category: Ponomarenko N]]
-
[[Category: Srajer, V.]]
+
[[Category: Srajer V]]
-
[[Category: BCB]]
+
-
[[Category: BPB]]
+
-
[[Category: FE2]]
+
-
[[Category: HEM]]
+
-
[[Category: LDA]]
+
-
[[Category: MQ7]]
+
-
[[Category: NS5]]
+
-
[[Category: SO4]]
+
-
[[Category: UQ2]]
+
-
[[Category: photosynthetic reaction center]]
+
-
[[Category: secondary quinone (qb)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:54 2008''
+

Current revision

PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)

PDB ID 1r2c

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools