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-Structure paper
タイトル | Crenactin forms actin-like double helical filaments regulated by arcadin-2. |
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ジャーナル・号・ページ | Elife, Vol. 5, Year 2016 |
掲載日 | 2016年11月17日 |
著者 | Thierry Izoré / Danguole Kureisaite-Ciziene / Stephen H McLaughlin / Jan Löwe / |
PubMed 要旨 | The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon supports the theory of a common origin of Crenarchaea and Eukaryotes. Monomeric structures of ...The similarity of eukaryotic actin to crenactin, a filament-forming protein from the crenarchaeon supports the theory of a common origin of Crenarchaea and Eukaryotes. Monomeric structures of crenactin and actin are similar, although their filament architectures were suggested to be different. Here we report that crenactin forms double helical filaments that show exceptional similarity to eukaryotic F-actin. With cryo-electron microscopy and helical reconstruction we solved the structure of the crenactin filament to 3.8 Å resolution. When forming double filaments, the 'hydrophobic plug' loop in crenactin rearranges. Arcadin-2, also encoded by the arcade gene cluster, binds tightly with its C-terminus to the hydrophobic groove of crenactin. Binding is reminiscent of eukaryotic actin modulators such as cofilin and thymosin β4 and arcadin-2 is a depolymeriser of crenactin filaments. Our work further supports the theory of shared ancestry of Eukaryotes and Crenarchaea. |
リンク | Elife / PubMed:27852434 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 1.6 - 3.8 Å |
構造データ | EMDB-4117, PDB-5mw1: PDB-5ly3: PDB-5ly5: |
化合物 | ChemComp-ADP: ChemComp-HOH: |
由来 |
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キーワード | STRUCTURAL PROTEIN / actin / bacterial cytoskeleton / UNKNOWN FUNCTION / arcade clauster / crenactin |