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[[Image:1all.gif|left|200px]]
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{{STRUCTURE_1all|  PDB=1all  |  SCENE=  }}
'''ALLOPHYCOCYANIN'''


==ALLOPHYCOCYANIN==
<StructureSection load='1all' size='340' side='right'caption='[[1all]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1all]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ALL 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]] 2.3&#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=MEN:N-METHYL+ASPARAGINE'>MEN</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=1all FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1all OCA], [https://pdbe.org/1all PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1all RCSB], [https://www.ebi.ac.uk/pdbsum/1all PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1all ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHAA_ARTPT PHAA_ARTPT] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers.
== 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/al/1all_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=1all ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phycobiliprotein allophycocyanin from the cyanobacterium Spirulina platensis has been isolated and crystallized. The crystals belong to space group P6(3)22 with cell constants a = b = 101.9 A, c = 130.6 A, alpha = beta = 90 degrees, gamma = 120 degrees, with one (alpha beta) monomer in the asymmetric unit. The three-dimensional structure of the (alpha beta) monomer was solved by multiple isomorphous replacement. The crystal structure has been refined in a cyclic manner by energy-restrained crystallographic refinement and model building. The conventional crystallographic R-factor of the final model is 19.6% with data from 8.0 to 2.3 A. The molecular structure of the subunits resembles other solved phycobiliprotein structures. In comparison to C-phycocyanin and b-phycoerythrin the major differences arise from deletions and insertions of segments involved in the protein-chromophore interactions. The stereochemistry of the alpha 84 and beta 84 chiral atoms are C(2)-R, C(3)-R and C(31)-R. The configuration (C(4)-Z, C(10)-Z and C(15)-Z) and the conformation (C(5)-anti, C(9)-syn and C(14)-anti) are equal for both chromophores.


==Overview==
Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution.,Brejc K, Ficner R, Huber R, Steinbacher S J Mol Biol. 1995 Jun 2;249(2):424-40. PMID:7783202<ref>PMID:7783202</ref>
The phycobiliprotein allophycocyanin from the cyanobacterium Spirulina platensis has been isolated and crystallized. The crystals belong to space group P6(3)22 with cell constants a = b = 101.9 A, c = 130.6 A, alpha = beta = 90 degrees, gamma = 120 degrees, with one (alpha beta) monomer in the asymmetric unit. The three-dimensional structure of the (alpha beta) monomer was solved by multiple isomorphous replacement. The crystal structure has been refined in a cyclic manner by energy-restrained crystallographic refinement and model building. The conventional crystallographic R-factor of the final model is 19.6% with data from 8.0 to 2.3 A. The molecular structure of the subunits resembles other solved phycobiliprotein structures. In comparison to C-phycocyanin and b-phycoerythrin the major differences arise from deletions and insertions of segments involved in the protein-chromophore interactions. The stereochemistry of the alpha 84 and beta 84 chiral atoms are C(2)-R, C(3)-R and C(31)-R. The configuration (C(4)-Z, C(10)-Z and C(15)-Z) and the conformation (C(5)-anti, C(9)-syn and C(14)-anti) are equal for both chromophores.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1ALL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ALL OCA].
</div>
<div class="pdbe-citations 1all" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Isolation, crystallization, crystal structure analysis and refinement of allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution., Brejc K, Ficner R, Huber R, Steinbacher S, J Mol Biol. 1995 Jun 2;249(2):424-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7783202 7783202]
*[[Allophycocyanin|Allophycocyanin]]
*[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Brejc, K.]]
[[Category: Brejc K]]
[[Category: Ficner, R.]]
[[Category: Ficner R]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher S]]
[[Category: Light-harvesting protein]]
[[Category: Phycobiliprotein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:25:36 2008''