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spinqualitylabelsall models 1jwy, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE DYNAMIN A GTPASE DOMAIN COMPLEXED WITH GDP, DETERMINED AS MYOSIN FUSION

Overview

Dynamins form a family of multidomain GTPases involved in endocytosis, vesicle trafficking and maintenance of mitochondrial morphology. In, contrast to the classical switch GTPases, a force-generating function has, been suggested for dynamins. Here we report the 2.3 A crystal structure of, the nucleotide-free and GDP-bound GTPase domain of Dictyostelium, discoideum dynamin A. The GTPase domain is the most highly conserved, region among dynamins. The globular structure contains the G-protein core, fold, which is extended from a six-stranded beta-sheet to an, eight-stranded one by a 55 amino acid insertion. This topologically unique, insertion distinguishes dynamins from other subfamilies of GTP-binding, proteins. An additional N-terminal helix interacts with the C-terminal, helix of the GTPase domain, forming a hydrophobic groove, which could be, occupied by C-terminal parts of dynamin not present in our construct. The, lack of major conformational changes between the nucleotide-free and the, GDP-bound state suggests that mechanochemical rearrangements in dynamin, occur during GTP binding, GTP hydrolysis or phosphate release and are not, linked to loss of GDP.

About this Structure

1JWY is a Protein complex structure of sequences from Dictyostelium discoideum with GLC, MG, ADP and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms., Niemann HH, Knetsch ML, Scherer A, Manstein DJ, Kull FJ, EMBO J. 2001 Nov 1;20(21):5813-21. PMID:11689422

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