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From Proteopedia
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== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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="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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1all" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Allophycocyanin|Allophycocyanin]] | *[[Allophycocyanin|Allophycocyanin]] | ||
*[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]] | *[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
ALLOPHYCOCYANIN
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