6r83

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'''Unreleased structure'''
 
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The entry 6r83 is ON HOLD until sometime in the future
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==CryoEM structure and molecular model of squid hemocyanin (Todarodes pacificus , TpH)==
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<SX load='6r83' size='340' side='right' viewer='molstar' caption='[[6r83]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6r83]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Todarodes_pacificus Todarodes pacificus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R83 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R83 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r83 OCA], [https://pdbe.org/6r83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r83 RCSB], [https://www.ebi.ac.uk/pdbsum/6r83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r83 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0P0UX03_TODPA A0A0P0UX03_TODPA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The oxygen transporter of molluscs, hemocyanin, consists of long pearl-necklace-like subunits of several globular domains. The subunits assemble in a complex manner to form cylindrical decamers. Typically, the first six domains of each subunit assemble together to form the cylinder wall, while the C-terminal domains form a collar that fills or caps the cylinder. During evolution, various molluscs have been able to fine-tune their oxygen binding by deleting or adding C-terminal domains and adjusting their inner-collar architecture. However, squids have duplicated one of the wall domains of their subunits instead. Here, using cryo-EM and an optimized refinement protocol implemented in SPHIRE, this work tackled the symmetry-mismatched structure of squid hemocyanin, revealing the precise effect of this duplication on its quaternary structure and providing a potential model for its structural evolution.
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Authors:
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Cryo-EM reveals the asymmetric assembly of squid hemocyanin.,Tanaka Y, Kato S, Stabrin M, Raunser S, Matsui T, Gatsogiannis C IUCrJ. 2019 Apr 5;6(Pt 3):426-437. doi: 10.1107/S205225251900321X. eCollection, 2019 May 1. PMID:31098023<ref>PMID:31098023</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6r83" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Todarodes pacificus]]
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[[Category: Gatsogiannis C]]
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[[Category: Kato S]]
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[[Category: Matsui T]]
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[[Category: Raunser S]]
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[[Category: Stabrin M]]
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[[Category: Tanaka Y]]

Current revision

CryoEM structure and molecular model of squid hemocyanin (Todarodes pacificus , TpH)

6r83, resolution 5.10Å

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