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TitleCryo-EM reveals the asymmetric assembly of squid hemocyanin.
Journal, issue, pagesIUCrJ, Vol. 6, Issue Pt 3, Page 426-437, Year 2019
Publish dateMay 1, 2019
AuthorsYoshikazu Tanaka / Sanae Kato / Markus Stabrin / Stefan Raunser / Takashi Matsui / Christos Gatsogiannis /
PubMed AbstractThe 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. ...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 , 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.
External linksIUCrJ / PubMed:31098023 / PubMed Central
MethodsEM (single particle)
Resolution5.1 Å
Structure data

4750

6r83

EMDB-4750, PDB-6r83:
CryoEM structure and molecular model of squid hemocyanin (Todarodes pacificus , TpH)
Method: EM (single particle) / Resolution: 5.1 Å

Source
  • todarodes pacificus (Japanese flying squid)
  • Japanese flying squid (Japanese flying squid)
KeywordsOXYGEN TRANSPORT / oxygen transporter / mollusc / hemocyanin / copper / symmetry mismatch

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