7AX3

CryoEM structure of the super-constricted two-start dynamin 1 filament

This is a non-PDB format compatible entry.

Summary for 7AX3

• Entry DOI: 10.2210/pdb7ax3/pdb
• EMDB information: 11932
• Descriptor: Dynamin-1, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION (3 entities in total)
• Functional Keywords: dynamin, cytosolic protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 36
• Total formula weight: 3530947.39

Authors

Liu, J.W.,Zhang, P.J. (deposition date: 2020-11-09, release date: 2021-11-10)

Primary citation

Liu, J.,Alvarez, F.J.D.,Clare, D.K.,Noel, J.K.,Zhang, P.
CryoEM structure of the super-constricted two-start dynamin 1 filament.
Nat Commun, 12:5393-5393, 2021

PubMed Abstract: Dynamin belongs to the large GTPase superfamily, and mediates the fission of vesicles during endocytosis. Dynamin molecules are recruited to the neck of budding vesicles to assemble into a helical collar and to constrict the underlying membrane. Two helical forms were observed: the one-start helix in the constricted state and the two-start helix in the super-constricted state. Here we report the cryoEM structure of a super-constricted two-start dynamin 1 filament at 3.74 Å resolution. The two strands are joined by the conserved GTPase dimeric interface. In comparison with the one-start structure, a rotation around Hinge 1 is observed, essential for communicating the chemical power of the GTPase domain and the mechanical force of the Stalk and PH domain onto the underlying membrane. The Stalk interfaces are well conserved and serve as fulcrums for adapting to changing curvatures. Relative to one-start, small rotations per interface accumulate to bring a drastic change in the helical pitch. Elasticity theory rationalizes the diversity of dynamin helical symmetries and suggests corresponding functional significance.

PubMed: 34518553
DOI: 10.1038/s41467-021-25741-x

Experimental method

ELECTRON MICROSCOPY (3.74 Å)