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1Y8M

Solution Structure of Yeast Mitochondria Fission Protein Fis1

Summary for 1Y8M
Entry DOI10.2210/pdb1y8m/pdb
Related1PC2
DescriptorFis1 (1 entity in total)
Functional Keywordsmitochondria, fission, unknown function
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationMitochondrion outer membrane; Single-pass membrane protein: P40515
Total number of polymer chains1
Total formula weight16725.08
Authors
Suzuki, M.,Youle, R.J.,Tjandra, N. (deposition date: 2004-12-13, release date: 2005-04-05, Last modification date: 2024-05-22)
Primary citationSuzuki, M.,Neutzner, A.,Tjandra, N.,Youle, R.J.
Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission.
J.Biol.Chem., 280:21444-21452, 2005
Cited by
PubMed Abstract: Mitochondrial fission is facilitated by a multiprotein complex assembled at the division site. The required components of the fission machinery in Saccharomyces cerevisiae include Dnm1, Fis1, and Mdv1. In the present study, we determined the protein structure of yeast Fis1 using NMR spectroscopy. Although the six alpha-helices, as well as their folding, in the yeast Fis1 structure are similar to those of the tetratricopeptide repeat (TPR) domains of the human Fis1 structure, the two structures differ in their N termini. The N-terminal tail of human Fis1 is flexible and unstructured, whereas a major segment of the longer N terminus of yeast Fis1 is fixed to the concave face formed by the six alpha-helices in the TPR domains. To investigate the role of the fixed N terminus, exogenous Fis1 was expressed in yeast lacking the endogenous protein. Expression of yeast Fis1 protein rescued mitochondrial fission in delta fis1 yeast only when the N-terminal TPR binding segment was left intact. The presence of this segment is also correlated to the recruitment of Mdv1 to mitochondria. The conformation of the N-terminal segment embedded in the TPR pocket indicates an intra-molecular regulation of Fis1 bioactivity. Although the TPR-like helix bundle of Fis1 mediates the interaction with Dnm1 and Mdv1, the N terminus of Fis1 is a prerequisite to recruit Mdv1 to facilitate mitochondrial fission.
PubMed: 15809300
DOI: 10.1074/jbc.M414092200
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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건을2025-07-09부터공개중

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