View source for 6yqg


==Crystal structure of native Phycocyanin in spacegroup P63 at 1.45 Angstroms.==
<StructureSection load='6yqg' size='340' side='right'caption='[[6yqg]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yqg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus Thermosynechococcus vestitus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YQG 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]] 1.45&#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>, <scene name='pdbligand=TE4:TETRACAINE'>TE4</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=6yqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yqg OCA], [https://pdbe.org/6yqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yqg RCSB], [https://www.ebi.ac.uk/pdbsum/6yqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yqg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHCA_THEVB PHCA_THEVB] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The unique crystallization properties of the antenna protein C-phycocyanin (C-PC) from the thermophilic cyanobacterium Thermosynechococcus elongatus are reported and discussed. C-PC crystallizes in hundreds of significantly different conditions within a broad pH range and in the presence of a wide variety of precipitants and additives. Remarkably, the crystal dimensions vary from a few micrometres, as used in serial crystallography, to several hundred micrometres, with a very diverse crystal morphology. More than 100 unique single-crystal X-ray diffraction data sets were collected from randomly selected crystals and analysed. The addition of small-molecule additives revealed three new crystal packings of C-PC, which are discussed in detail. The high propensity of this protein to crystallize, combined with its natural blue colour and its fluorescence characteristics, make it an excellent candidate as a superior and highly adaptable model system in crystallography. C-PC can be used in technical and methods development approaches for X-ray and neutron diffraction techniques, and as a system for comprehending the fundamental principles of protein crystallography.

C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening.,Sarrou I, Feiler CG, Falke S, Peard N, Yefanov O, Chapman H Acta Crystallogr D Struct Biol. 2021 Feb 1;77(Pt 2):224-236. doi: , 10.1107/S2059798320016071. Epub 2021 Jan 26. PMID:33559611<ref>PMID:33559611</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yqg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phycocyanin|Phycocyanin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermosynechococcus vestitus]]
[[Category: Falke S]]
[[Category: Feiler CG]]
[[Category: Sarrou I]]