Imperial College London
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DrHarryLow

Faculty of Medicine, Department of Infectious Disease

Senior Wellcome Trust Fellow and Proleptic Reader
 
 
 
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Contact

 

+44 (0)20 7594 3064h.low

 
 
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Location

 

260Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Bohuszewicz:2018:10.1038/s41594-018-0097-6,
author = {Bohuszewicz, O and Low, HH},
doi = {10.1038/s41594-018-0097-6},
journal = {Nature Structural and Molecular Biology},
pages = {722--731},
title = {Structure of a mitochondrial fission dynamin in the closed conformation},
url = {http://dx.doi.org/10.1038/s41594-018-0097-6},
volume = {25},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of a mitochondrial fission dynamin (CmDnm1) from the algae Cyanidioschyzon merolae. Unlike other eukaryotic dynamin structures, CmDnm1 is in a hinge 1 closed conformation, with the GTPase domain compacted against the stalk. Within the crystal, CmDnm1 packs as a diamond-shaped tetramer that is consistent with an inactive off-membrane state. Crosslinking, photoinduced electron transfer assays, and electron microscopy verify these structures. In vitro, CmDnm1 forms concentration-dependent rings and protein–lipid tubes reminiscent of DNM1-L and classical dynamin with hinge 1 open. Our data provides a mechanism for filament collapse and membrane release that may extend to other dynamin family members. Additionally, hinge 1 closing may represent a key conformational change that contributes to membrane fission.
AU  - Bohuszewicz,O
AU  - Low,HH
DO  - 10.1038/s41594-018-0097-6
EP  - 731
PY  - 2018///
SN  - 1545-9985
SP  - 722
TI  - Structure of a mitochondrial fission dynamin in the closed conformation
T2  - Nature Structural and Molecular Biology
UR  - http://dx.doi.org/10.1038/s41594-018-0097-6
UR  - http://hdl.handle.net/10044/1/62207
VL  - 25
ER  -
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