5MW1

cryoEM structure of crenactin double helical filament at 3.8A resolution

Replaces:  5LY4

Summary for 5MW1

• Entry DOI: 10.2210/pdb5mw1/pdb
• EMDB information: 4117
• Descriptor: Actin/actin family protein, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: actin, bacterial cytoskeleton, structural protein
• Biological source: Pyrobaculum calidifontis
• Total number of polymer chains: 6
• Total formula weight: 293116.11

Authors

Izore, T.,Lowe, J. (deposition date: 2017-01-17, release date: 2017-02-08, Last modification date: 2024-05-08)

Primary citation

Izore, T.,Kureisaite-Ciziene, D.,McLaughlin, S.H.,Lowe, J.
Crenactin forms actin-like double helical filaments regulated by arcadin-2.
Elife, 5:-, 2016

PubMed Abstract: 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.

PubMed: 27852434
DOI: 10.7554/eLife.21600

Experimental method

ELECTRON MICROSCOPY (3.8 Å)