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Cryo-EM reveals the asymmetric assembly of squid hemocyanin.

ABSTRACT: 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.

SUBMITTER: Tanaka Y

PROVIDER: S-EPMC6503924 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

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Cryo-EM reveals the asymmetric assembly of squid hemocyanin.

Tanaka Yoshikazu Y Kato Sanae S Stabrin Markus M Raunser Stefan S Matsui Takashi T Gatsogiannis Christos C

IUCrJ 20190405 Pt 3

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 adjust ...[more]

PMID: 31098023

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