Abstract
Fis1 mediates mitochondrial and peroxisomal fission. It is tail-anchored to these organelles by a transmembrane domain, exposing a soluble cytoplasmic domain. Previous studies suggested that Fis1 is autoinhibited by its N-terminal region. Here, a 1.75 Å resolution crystal structure of the Fis1 cytoplasmic domain from Saccharomyces cerevisiae is reported which adopts a tetratricopeptide-repeat fold. It is observed that this fold creates a concave surface important for fission, but is sterically occluded by its N-terminal region. Thus, this structure provides a physical basis for autoinhibition and allows a detailed examination of the interactions that stabilize the inhibited state of this molecule.
Original language | English (US) |
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Pages (from-to) | 1310-1315 |
Number of pages | 6 |
Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
Volume | 67 |
Issue number | 11 |
DOIs | |
State | Published - Nov 2011 |
Keywords
- membrane dynamics
- mitochondria
- peroxisomes
- protein-protein interactions
- tail-anchoring
- tetratricopeptide repeats
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Structural Biology
- Genetics
- Condensed Matter Physics