3ZVR

Crystal structure of Dynamin

Summary for 3ZVR

• Entry DOI: 10.2210/pdb3zvr/pdb
• Related: 2AKA
• Descriptor: DYNAMIN-1, PENTAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: hydrolase, drp1, drp, endocytosis, mitochondrial fission, gtpase, stalk, ph, bse, membrane fission
• Biological source: RATTUS NORVEGICUS (NORWAY RAT)
• Cellular location: Cytoplasm. Isoform 2: Cytoplasm. Isoform 6: Cytoplasm: P21575
• Total number of polymer chains: 1
• Total formula weight: 89077.47

Authors

Ford, M.G.J.,Jenni, S.,Nunnari, J. (deposition date: 2011-07-27, release date: 2011-09-21, Last modification date: 2023-12-20)

Primary citation

Ford, M.G.J.,Jenni, S.,Nunnari, J.
The Crystal Structure of Dynamin
Nature, 477:561-, 2011

PubMed Abstract: Dynamin-related proteins (DRPs) are multi-domain GTPases that function via oligomerization and GTP-dependent conformational changes to play central roles in regulating membrane structure across phylogenetic kingdoms. How DRPs harness self-assembly and GTP-dependent conformational changes to remodel membranes is not understood. Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state. The dynamin 1 monomer is an extended structure with the GTPase domain and bundle signalling element positioned on top of a long helical stalk with the pleckstrin homology domain flexibly attached on its opposing end. Dynamin 1 dimer and higher order dimer multimers form via interfaces located in the stalk. Analysis of these interfaces provides insight into DRP family member specificity and regulation and provides a framework for understanding the biogenesis of higher order DRP structures and the mechanism of DRP-mediated membrane scission events.

PubMed: 21927001
DOI: 10.1038/NATURE10441

Experimental method

X-RAY DIFFRACTION (3.1 Å)