1pc2
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Solution structure of human mitochondria fission protein Fis1
OverviewOverview
Fis1 in yeast localizes to the outer mitochondrial membrane and, facilitates mitochondrial fission by forming protein complexes with Dnm1, and Mdv1. Fis1 orthologs exist in higher eukaryotes, suggesting that they, are functionally conserved. In the present study, we cloned the human Fis1, ortholog that was predicted in a database, and determined the protein, structure using NMR spectroscopy. Following a flexible N-terminal tail, six alpha-helices connected with short loops construct a single core, domain. The C-terminal tail containing a transmembrane segment appears to, be disordered. In the core domain, each of two sequentially adjacent, helices forms a hairpin-like conformation, resulting in a six helix, assembly forming a slightly twisted slab similar to that of a tandem array, of tetratrico-peptide repeat (TPR) motif folds. Within this TPR-like core, domain, no significant sequence similarity to the typical TPR motif is, found. The structural analogy to the TPR-containing proteins suggests that, Fis1 binds to other proteins at its concave hydrophobic surface. A simple, composition of Fis1 comprised of a binding domain and a transmembrane, segment indicates that the protein may function as a molecular adaptor on, the mitochondrial outer membrane. In HeLa cells, however, increased levels, in mitochondria-associated Fis1 did not result in mitochondrial, translocation of Drp1, a potential binding partner of Fis1 implicated in, the regulation of mitochondrial fission, suggesting that the interaction, between Drp1 and Fis1 is regulated.
About this StructureAbout this Structure
1PC2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle., Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N, J Mol Biol. 2003 Nov 28;334(3):445-58. PMID:14623186
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