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-Structure paper
| タイトル | Structure of mega-hemocyanin reveals protein origami in snails. |
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| ジャーナル・号・ページ | Structure, Vol. 23, Issue 1, Page 93-9103, Year 2015 |
| 掲載日 | 2015年1月6日 |
著者 | Christos Gatsogiannis / Oliver Hofnagel / Jürgen Markl / Stefan Raunser / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:25482543 |
| 手法 | EM (単粒子) |
| 解像度 | 10.4 - 12.2 Å |
| 構造データ | ![]() EMDB-6185: ![]() EMDB-6186: |
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Melanoides tuberculata (無脊椎動物)