Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
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Author / Creator
Yan, Liming , Qi, Yuanbo , Huang, Xiaofang , Yu, Caiting , Lan, Lan , Guo, Xiangyang , Rao, Zihe , Hu, Junjie and Lou, Zhiyong
Publisher
New York: Nature Publishing Group US
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Language
English
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Publisher
New York: Nature Publishing Group US
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Contents
Fusion of the outer mitochondrial membrane is mediated by the dynamin-like GTPase mitofusin (MFN). Here, we determined the structure of the minimal GTPase domain (MGD) of human MFN1 in complex with GDP-BeF
3
–
. The MGD folds into a canonical GTPase fold with an associating four-helix bundle, HB1, and forms a dimer. A potassium ion in the...
Alternative Titles
Full title
Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
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Record Identifier
TN_cdi_proquest_miscellaneous_2008885837
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2008885837
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/s41594-018-0034-8
