This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2rcr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2rcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rcr, resolution 3.1&Aring;" /> '''STRUCTURE OF THE MEMB...)
Current revision (09:21, 21 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2rcr.jpg|left|200px]]<br /><applet load="2rcr" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2rcr, resolution 3.1&Aring;" />
 
-
'''STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES'''<br />
 
-
==Overview==
+
==STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES==
-
The structure of the photosynthetic reaction center (RC) from Rhodobacter, sphaeroides was determined at 3.1-A resolution by the molecular, replacement method, using the Rhodopseudomonas viridis RC as the search, structure. Atomic coordinates were refined with the difference Fourier, method and restrained least-squares refinement techniques to a current R, factor of 22%. The tertiary structure of the RC complex is stabilized by, hydrophobic interactions between the L and M chains, by interactions of, the pigments with each other and with the L and M chains, by residues from, the L and M chains that coordinate to the Fe2+, by salt bridges that are, formed between the L and M chains and the H chain, and possibly by, electrostatic forces between the ends of helices. The conserved residues, at the N-termini of the L and M chains were identified as recognition, sites for the H chain.
+
<StructureSection load='2rcr' size='340' side='right'caption='[[2rcr]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[2rcr]] 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=2RCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCR FirstGlance]. <br>
-
2RCR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE, BCL, BPH and UQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2RCR OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</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=UQ:COENZYME+Q10,+(2Z,6E,10Z,14E,18E,22E,26Z)-ISOMER'>UQ</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcr OCA], [https://pdbe.org/2rcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcr RCSB], [https://www.ebi.ac.uk/pdbsum/2rcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcr ProSAT]</span></td></tr>
-
Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides., Chang CH, el-Kabbani O, Tiede D, Norris J, Schiffer M, Biochemistry. 1991 Jun 4;30(22):5352-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2036404 2036404]
+
</table>
-
[[Category: Protein complex]]
+
== Function ==
-
[[Category: Rhodobacter sphaeroides]]
+
[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.
-
[[Category: Chang, C.H.]]
+
== Evolutionary Conservation ==
-
[[Category: Norris, J.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Schiffer, M.]]
+
Check<jmol>
-
[[Category: BCL]]
+
<jmolCheckbox>
-
[[Category: BPH]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/2rcr_consurf.spt"</scriptWhenChecked>
-
[[Category: FE]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: UQ]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: photosynthetic reaction center]]
+
</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=2rcr ConSurf].
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:57:16 2007''
+
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Cereibacter sphaeroides]]
 +
[[Category: Large Structures]]
 +
[[Category: Chang C-H]]
 +
[[Category: Norris J]]
 +
[[Category: Schiffer M]]

Current revision

STRUCTURE OF THE MEMBRANE-BOUND PROTEIN PHOTOSYNTHETIC REACTION CENTER FROM RHODOBACTER SPHAEROIDES

PDB ID 2rcr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rcr"
Personal tools