AI Article Synopsis
- Fis1 is a protein that helps with the division of mitochondria and peroxisomes, anchored to these organelles by a specific domain and having a soluble portion that interacts with the cytoplasm.
- New research has revealed a detailed crystal structure of the cytoplasmic domain of Fis1 from yeast, showing that it has a unique shape called a tetratricopeptide-repeat fold.
- This structure highlights how the N-terminal region of Fis1 blocks the active site, explaining why Fis1 is autoinhibited and allowing for further study of its interactions in this inactive form.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212442 | PMC |
| http://dx.doi.org/10.1107/S1744309111029368 | DOI Listing |
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