TY - JOUR
T1 - Cryo-EM reveals the asymmetric assembly of squid hemocyanin
AU - Tanaka, Yoshikazu
AU - Kato, Sanae
AU - Stabrin, Markus
AU - Raunser, Stefan
AU - Matsui, Takashi
AU - Gatsogiannis, Christos
N1 - Funding Information:
This work was supported by the Max Planck Society, the Deutsche Forschungsgemeinschaft (grant No. FOR1905), Presto (YT), and the Japan Society for the Promotion of Science [Kakenhi Grant Nos 26291008, 24000011, 15 K K0248, 16 H00748 (YT) and 17 K07942 (SK)].
Publisher Copyright:
© Yoshikazu Tanaka et al. 2019.
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
KW - cryo-electron microscopy
KW - macromolecular machines
KW - protein structures
KW - single-particle cryo-EM
KW - structure determination
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U2 - 10.1107/S205225251900321X
DO - 10.1107/S205225251900321X
M3 - Article
AN - SCOPUS:85065294094
SN - 2052-2525
VL - 6
SP - 426
EP - 437
JO - IUCrJ
JF - IUCrJ
ER -