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TitleStructure of mega-hemocyanin reveals protein origami in snails.
Journal, issue, pagesStructure, Vol. 23, Issue 1, Page 93-9103, Year 2015
Publish dateJan 6, 2015
AuthorsChristos Gatsogiannis / Oliver Hofnagel / Jürgen Markl / Stefan Raunser /
PubMed AbstractMega-hemocyanin is a 13.5 MDa oxygen transporter found in the hemolymph of some snails. Similar to typical gastropod hemocyanins, it is composed of 400 kDa building blocks but has additional ...Mega-hemocyanin is a 13.5 MDa oxygen transporter found in the hemolymph of some snails. Similar to typical gastropod hemocyanins, it is composed of 400 kDa building blocks but has additional 550 kDa subunits. Together, they form a large, completely filled cylinder. The structural basis for this highly complex protein packing is not known so far. Here, we report the electron cryomicroscopy (cryo-EM) structure of mega-hemocyanin complexes from two different snail species. The structures reveal that mega-hemocyanin is composed of flexible building blocks that differ in their conformation, but not in their primary structure. Like a protein origami, these flexible blocks are optimally packed, implementing different local symmetries and pseudosymmetries. A comparison between the two structures suggests a surprisingly simple evolutionary mechanism leading to these large oxygen transporters.
External linksStructure / PubMed:25482543
MethodsEM (single particle)
Resolution10.4 - 12.2 Å
Structure data

EMDB-6185:
Electron cryo-microscopy of Melanoides tuberculata mega-hemocyanin
Method: EM (single particle) / Resolution: 12.2 Å

EMDB-6186:
Electron cryo-microscopy of Terebralia palustris mega-hemocyanin
Method: EM (single particle) / Resolution: 10.4 Å

Source
  • Melanoides tuberculata (invertebrata)
  • Terebralia palustris (invertebrata)

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