View source for 5tou


==STRUCTURE OF C-PHYCOCYANIN FROM ARCTIC PSEUDANABAENA SP. LW0831==
<StructureSection load='5tou' size='340' side='right'caption='[[5tou]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tou]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudanabaena_sp._lw0831 Pseudanabaena sp. lw0831]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TOU 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]] 2.04&#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=5tou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tou OCA], [https://pdbe.org/5tou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tou RCSB], [https://www.ebi.ac.uk/pdbsum/5tou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tou ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/V5NXI0_9CYAN V5NXI0_9CYAN] 
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== Publication Abstract from PubMed ==
The cold adaptation mechanism of phycobiliproteins, the major photosynthetic pigment-proteins in cyanobacteria and red algae, has rarely been studied. Here we reported the biochemical, structural, and molecular dynamics simulation study of the C-phycocyanin from Arctic cyanobacterial strain Pseudanabaena sp. LW0831. We characterized the phycobilisome components of LW0831 and obtained their gene sequences. Compared to the mesophilic counterpart from Arthrospira platensis (Ar-C-PC), LW0831 C-phycocyanin (Ps-C-PC) has a decreased thermostability (Tm of -16 degrees C), one of the typical features of cold-adapted enzymes. To uncover its structural basis, we resolved the crystal structure of Ps-C-PC 1 at 2.04A. Consistent with the decrease in thermostability, comparative structural analyses revealed decreased intra-trimer and inter-trimer interactions in Ps-C-PC 1, compared to Ar-C-PC. However, comparative molecular dynamics simulations indicated that Ps-C-PC 1 shows similar flexibilities to Ar-C-PC for both the (alphabeta)3 trimer and (alphabeta)6 hexamer. Therefore, the optimization mode is clearly different from cold-adapted enzymes, which usually have increased flexibilities. Detailed analyses demonstrated different optimization modes for the alpha and beta subunits and it was revealed that hydrophobic interactions are key to this difference, though salt bridges, hydrogen bonds, and surface hydrophobicity are also involved. This study is the first report of the structure of cold-adapted phycobiliproteins and provides insights into the cold-adaptation strategies of non-enzyme proteins.

Structural insights into the cold adaptation of the photosynthetic pigment-protein C-phycocyanin from an Arctic cyanobacterium.,Su HN, Wang QM, Li CY, Li K, Luo W, Chen B, Zhang XY, Qin QL, Zhou BC, Chen XL, Zhang YZ, Xie BB Biochim Biophys Acta. 2017 Apr;1858(4):325-335. doi:, 10.1016/j.bbabio.2017.02.004. Epub 2017 Feb 7. PMID:28188780<ref>PMID:28188780</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5tou" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phycocyanin|Phycocyanin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudanabaena sp. lw0831]]
[[Category: Li CY]]
[[Category: Su HN]]
[[Category: Wang QM]]
[[Category: Xie BB]]
[[Category: Zhang YZ]]