The 1.75 Å resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain

James E. Tooley, Victor Khangulov, Jonathan P.B. Lees, Jamie L. Schlessman, Maria C. Bewley, Annie Heroux, Jürgen Bosch, R. Blake Hill

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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 languageEnglish (US)
Pages (from-to)1310-1315
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number11
DOIs
Publication statusPublished - Nov 1 2011

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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