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Structure paper

TitleA pseudoatomic model of the dynamin polymer identifies a hydrolysis-dependent powerstroke.
Journal, issue, pagesCell, Vol. 147, Issue 1, Page 209-222, Year 2011
Publish dateSep 30, 2011
AuthorsJoshua S Chappie / Jason A Mears / Shunming Fang / Marilyn Leonard / Sandra L Schmid / Ronald A Milligan / Jenny E Hinshaw / Fred Dyda /
PubMed AbstractThe 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 ...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.
External linksCell / PubMed:21962517 / PubMed Central
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.2 - 12.2 Å
Structure data

1949

3zys

EMDB-1949, PDB-3zys:
Human dynamin 1 deltaPRD polymer stabilized with GMPPCP
Method: EM (helical sym.) / Resolution: 12.2 Å

PDB-3zyc:
DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-GCP:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsHYDROLASE / MEMBRANE FISSION / NUCLEOTIDE-BINDING / ENDOCYTOSIS / MOTOR PROTEIN / HYDROLASE/GTP-BINDING PROTEIN / HYDROLASE-GTP-BINDING PROTEIN COMPLEX / GTP HYDROLYSIS / MEMBRANE REMODELING

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