PDBsum entry 3snh

Endocytosis

PDB id: 3snh

Contents

Protein chain

652 a.a.

PDB id:

3snh

Name:

Endocytosis

Title:

Crystal structure of nucleotide-free human dynamin1

Structure:

Dynamin-1. Chain: a. Fragment: unp residues 6-746. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dnm, dnm1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.70Å R-factor: 0.290 R-free: 0.331

Authors:

K.Faelber,O.Daumke

Key ref:

K.Faelber et al. (2011). Crystal structure of nucleotide-free dynamin. Nature, 477, 556-560. PubMed id: 21927000

Date:

29-Jun-11 Release date: 21-Sep-11

Protein chain

Q05193  (DYN1_HUMAN) -  Dynamin-1 from Homo sapiens

Seq: 864 a.a.

Struc: 652 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.6.5.5 - dynamin GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Nature 477:556-560 (2011)

PubMed id: 21927000

Crystal structure of nucleotide-free dynamin.

K.Faelber, Y.Posor, S.Gao, M.Held, Y.Roske, D.Schulze, V.Haucke, F.Noé, O.Daumke.

ABSTRACT

Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.