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New page: left|200px<br /><applet load="1lia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lia, resolution 2.8Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1lia.gif|left|200px]]<br /><applet load="1lia" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lia, resolution 2.8&Aring;" />
'''CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION==
The structure of R-phycoerythrin (R-PE) from Polysiphonia urceolata was, determined at 2.8 A resolution. The crystals belong to space group R3 with, unit cell dimensions of a = b = 189.8 A, c = 60.1 A. The subunit, composition of R-PE is (alpha 2 beta 2)3 gamma. The three-dimensional, structure of R-PE was solved by the multiple isomorphous replacement, method. After several cycles of model building and refinement, the, crystallographic R-factor of the final model is 18.0% with data from 10.0, to 2.8 A resolution. The four phycoerythrobilin chromophores alpha 84, alpha 140a, beta 84 and beta 155 in an (alpha beta) unit are each, covalently bound to a cysteine residue through ring A. The phycourobilin, chromophore is bound to cysteine beta 50 by ring A and bound to cysteine, beta 61 by ring D. The ring A and ring D of phycourobilin deviate from the, conjugate plane formed by ring B and ring C and the four rings form a, boat-shaped structure. R-PE contains a 34 kDa gamma subunit that is, assumed to lie in the central channel of the molecular disc (alpha 2 beta, 2)3. The energy transfer and relationship between cysteine residues and, chromophores are discussed.
<StructureSection load='1lia' size='340' side='right'caption='[[1lia]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lia]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Polysiphonia_urceolata Polysiphonia urceolata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LIA 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</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=1lia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lia OCA], [https://pdbe.org/1lia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lia RCSB], [https://www.ebi.ac.uk/pdbsum/1lia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lia ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHEA_POLUR PHEA_POLUR]
== 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/li/1lia_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=1lia ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of R-phycoerythrin (R-PE) from Polysiphonia urceolata was determined at 2.8 A resolution. The crystals belong to space group R3 with unit cell dimensions of a = b = 189.8 A, c = 60.1 A. The subunit composition of R-PE is (alpha 2 beta 2)3 gamma. The three-dimensional structure of R-PE was solved by the multiple isomorphous replacement method. After several cycles of model building and refinement, the crystallographic R-factor of the final model is 18.0% with data from 10.0 to 2.8 A resolution. The four phycoerythrobilin chromophores alpha 84, alpha 140a, beta 84 and beta 155 in an (alpha beta) unit are each covalently bound to a cysteine residue through ring A. The phycourobilin chromophore is bound to cysteine beta 50 by ring A and bound to cysteine beta 61 by ring D. The ring A and ring D of phycourobilin deviate from the conjugate plane formed by ring B and ring C and the four rings form a boat-shaped structure. R-PE contains a 34 kDa gamma subunit that is assumed to lie in the central channel of the molecular disc (alpha 2 beta 2)3. The energy transfer and relationship between cysteine residues and chromophores are discussed.


==About this Structure==
Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution.,Chang WR, Jiang T, Wan ZL, Zhang JP, Yang ZX, Liang DC J Mol Biol. 1996 Oct 11;262(5):721-31. PMID:8876649<ref>PMID:8876649</ref>
1LIA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Polysiphonia_urceolata Polysiphonia urceolata] with CYC and PUB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LIA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution., Chang WR, Jiang T, Wan ZL, Zhang JP, Yang ZX, Liang DC, J Mol Biol. 1996 Oct 11;262(5):721-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8876649 8876649]
</div>
<div class="pdbe-citations 1lia" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Polysiphonia urceolata]]
[[Category: Polysiphonia urceolata]]
[[Category: Protein complex]]
[[Category: Chang WR]]
[[Category: Chang, W.R.]]
[[Category: Jiang T]]
[[Category: Jiang, T.]]
[[Category: Liang DC]]
[[Category: Liang, D.C.]]
[[Category: CYC]]
[[Category: PUB]]
[[Category: light harvesting protein]]
 
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Latest revision as of 05:31, 5 June 2024

CRYSTAL STRUCTURE OF R-PHYCOERYTHRIN FROM POLYSIPHONIA AT 2.8 A RESOLUTION

1lia, resolution 2.80Å

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