Abstract
Biochemical and structural studies of dynamin have shown that the C-terminus of the GTPase effector domain (GED) folds back and docks onto a platform created by the N- and C-terminal α-helices of the GTPase domain to form a three-helix bundle. While cross-linking studies suggested that insect cell-expressed dynamin existed as a domain-swapped dimer, X-ray structures of protein expressed in Escherichia coli failed to detect evidence of this domain swap. Here, by cross-linking several cysteine pair replacements and analyzing cross-linked species by matrix-assisted laser desorption ionization Mega time of flight, we conclude that dynamin is not domain-swapped and that GED-GTPase domain interactions occur in cis.
Original language | English (US) |
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Pages (from-to) | 5724-5726 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 53 |
Issue number | 36 |
DOIs | |
State | Published - Sep 16 2014 |
ASJC Scopus subject areas
- Biochemistry