title: The 1.75 Å resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain.
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.
authors.affiliation: Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: James E
authors.initials: JE
authors.lastname: Tooley
authors.forename: Victor
authors.initials: V
authors.lastname: Khangulov
authors.forename: Jonathan P B
authors.initials: JP
authors.lastname: Lees
authors.forename: Jamie L
authors.initials: JL
authors.lastname: Schlessman
authors.forename: Maria C
authors.initials: MC
authors.lastname: Bewley
authors.forename: Annie
authors.initials: A
authors.lastname: Heroux
authors.forename: Jürgen
authors.initials: J
authors.lastname: Bosch
authors.forename: R Blake
authors.initials: RB
authors.lastname: Hill
mesh_terms: D018360:Crystallography, X-Ray; D024101:Mitochondrial Proteins / Q000737:chemistry*; D008958:Models, Molecular; D054730:Protein Interaction Domains and Motifs; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D040681:Structural Homology, Protein
chemical_list: C464859:FIS1 protein, S cerevisiae; D024101:Mitochondrial Proteins; D029701:Saccharomyces cerevisiae Proteins
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