3o48
From Proteopedia
Crystal structure of fission protein Fis1 from Saccharomyces cerevisiae
Structural highlights
Function[FIS1_YEAST] Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.[1] [2] [3] [4] Publication Abstract from PubMedFis1 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 A 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. The 1.75 A resolution structure of fission protein Fis1 from Saccharomyces cerevisiae reveals elusive interactions of the autoinhibitory domain.,Tooley JE, Khangulov V, Lees JP, Schlessman JL, Bewley MC, Heroux A, Bosch J, Hill RB Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt, 11):1310-5. Epub 2011 Oct 25. PMID:22102223[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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