6R83
CryoEM structure and molecular model of squid hemocyanin (Todarodes pacificus , TpH)
This is a non-PDB format compatible entry.
Summary for 6R83
| Entry DOI | 10.2210/pdb6r83/pdb |
| EMDB information | 4750 |
| Descriptor | Hemocyanin subunit 1 (1 entity in total) |
| Functional Keywords | oxygen transporter, mollusc, hemocyanin, copper, symmetry mismatch, oxygen transport |
| Biological source | Todarodes pacificus (Japanese flying squid) |
| Total number of polymer chains | 10 |
| Total formula weight | 3797411.88 |
| Authors | Tanaka, Y.,Kato, S.,Stabrin, M.,Raunser, S.,Matsui, T.,Gatsogiannis, C. (deposition date: 2019-03-31, release date: 2019-05-08, Last modification date: 2024-05-22) |
| Primary citation | Tanaka, Y.,Kato, S.,Stabrin, M.,Raunser, S.,Matsui, T.,Gatsogiannis, C. Cryo-EM reveals the asymmetric assembly of squid hemocyanin. Iucrj, 6:426-437, 2019 Cited by PubMed 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 , 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. PubMed: 31098023DOI: 10.1107/S205225251900321X PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.1 Å) |
Structure validation
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