6r83
From Proteopedia
(Difference between revisions)
| Line 7: | Line 7: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r83 OCA], [http://pdbe.org/6r83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r83 RCSB], [http://www.ebi.ac.uk/pdbsum/6r83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r83 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r83 OCA], [http://pdbe.org/6r83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r83 RCSB], [http://www.ebi.ac.uk/pdbsum/6r83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r83 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6r83" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:43, 29 May 2019
CryoEM structure and molecular model of squid hemocyanin (Todarodes pacificus , TpH)
| |||||||||||
