3ZYS

Human dynamin 1 deltaPRD polymer stabilized with GMPPCP

Summary for 3ZYS

• Entry DOI: 10.2210/pdb3zys/pdb
• Related: 1DYN 2DYN 2X2E 2X2F 3ZYC
• EMDB information: 1949
• Descriptor: DYNAMIN-1, INTERFERON-INDUCED GTP-BINDING PROTEIN MX1 (3 entities in total)
• Functional Keywords: hydrolase-gtp-binding protein complex, endocytosis, gtp hydrolysis, membrane remodeling, hydrolase/gtp-binding protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 6
• Total formula weight: 256905.02

Authors

Chappie, J.S.,Mears, J.A.,Fang, S.,Leonard, M.,Schmid, S.L.,Milligan, R.A.,Hinshaw, J.E.,Dyda, F. (deposition date: 2011-08-24, release date: 2011-10-12, Last modification date: 2024-05-08)

Primary citation

Chappie, J.S.,Mears, J.A.,Fang, S.,Leonard, M.,Schmid, S.L.,Milligan, R.A.,Hinshaw, J.E.,Dyda, F.
A Pseudoatomic Model of the Dynamin Polymer Identifies a Hydrolysis-Dependent Powerstroke.
Cell(Cambridge,Mass.), 147:209-, 2011

PubMed Abstract: The GTPase dynamin catalyzes membrane fission by forming a collar around the necks of clathrin-coated pits, but the specific structural interactions and conformational changes that drive this process remain a mystery. We present the GMPPCP-bound structures of the truncated human dynamin 1 helical polymer at 12.2 Å and a fusion protein, GG, linking human dynamin 1's catalytic G domain to its GTPase effector domain (GED) at 2.2 Å. The structures reveal the position and connectivity of dynamin fragments in the assembled structure, showing that G domain dimers only form between tetramers in sequential rungs of the dynamin helix. Using chemical crosslinking, we demonstrate that dynamin tetramers are made of two dimers, in which the G domain of one molecule interacts in trans with the GED of another. Structural comparison of GG(GMPPCP) to the GG transition-state complex identifies a hydrolysis-dependent powerstroke that may play a role in membrane-remodeling events necessary for fission.

PubMed: 21962517
DOI: 10.1016/J.CELL.2011.09.003

Experimental method

ELECTRON MICROSCOPY (12.2 Å)