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[[Image:1b8d.gif|left|200px]]<br /><applet load="1b8d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b8d, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN==
<StructureSection load='1b8d' size='340' side='right'caption='[[1b8d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1b8d]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Griffithsia_monilis Griffithsia monilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B8D 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene>, <scene name='pdbligand=PUB:PHYCOUROBILIN'>PUB</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=1b8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8d OCA], [https://pdbe.org/1b8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b8d RCSB], [https://www.ebi.ac.uk/pdbsum/1b8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b8d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHEA_GRIMO PHEA_GRIMO]
== 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/b8/1b8d_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=1b8d ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions alpha82 and alpha139. The beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues beta82 and beta158 and one phycourobilin covalently attached to rings A and D at residues beta50 and beta61, respectively. The electron density of the gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry, but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two tyrosine residues of the gamma-polypeptide are in close proximity to the phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer. Possible energy transfer pathways are discussed briefly.
The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions alpha82 and alpha139. The beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues beta82 and beta158 and one phycourobilin covalently attached to rings A and D at residues beta50 and beta61, respectively. The electron density of the gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry, but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two tyrosine residues of the gamma-polypeptide are in close proximity to the phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer. Possible energy transfer pathways are discussed briefly.


==About this Structure==
Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution.,Ritter S, Hiller RG, Wrench PM, Welte W, Diederichs K J Struct Biol. 1999 Jun 15;126(2):86-97. PMID:10388620<ref>PMID:10388620</ref>
1B8D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Griffithsia_monilis Griffithsia monilis] with <scene name='pdbligand=PEB:'>PEB</scene> and <scene name='pdbligand=PUB:'>PUB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8D OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution., Ritter S, Hiller RG, Wrench PM, Welte W, Diederichs K, J Struct Biol. 1999 Jun 15;126(2):86-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10388620 10388620]
</div>
<div class="pdbe-citations 1b8d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Griffithsia monilis]]
[[Category: Griffithsia monilis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Diederichs, K.]]
[[Category: Diederichs K]]
[[Category: Hiller, R G.]]
[[Category: Hiller RG]]
[[Category: Ritter, S.]]
[[Category: Ritter S]]
[[Category: Welte, W.]]
[[Category: Welte W]]
[[Category: Wrench, P M.]]
[[Category: Wrench PM]]
[[Category: PEB]]
[[Category: PUB]]
[[Category: light-harvesting complex]]
[[Category: phycobiliprotein]]
[[Category: red algae]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:34 2008''

Latest revision as of 05:37, 9 August 2023

CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN

1b8d, resolution 1.90Å

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