The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer

Chen, Kai-En, Richards, Ayanthi A., Arrifin, Juliana K., Ross, Ian L., Sweet, Matthew J., Kellie, Stuart, Kobe, Bostjan and Martin, Jennifer L. (2012) The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer. Acta Crystallographica Section D: Biological Crystallography, 68 6: 637-648. doi:10.1107/S0907444912006592

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Author Chen, Kai-En
Richards, Ayanthi A.
Arrifin, Juliana K.
Ross, Ian L.
Sweet, Matthew J.
Kellie, Stuart
Kobe, Bostjan
Martin, Jennifer L.
Title The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2012-06
Sub-type Article (original research)
DOI 10.1107/S0907444912006592
Open Access Status File (Author Post-print)
Volume 68
Issue 6
Start page 637
End page 648
Total pages 12
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell Publishing
Collection year 2013
Language eng
Formatted abstract
Fam96a mRNA, which encodes a mammalian DUF59 protein, is enriched in macrophages. Recombinant human Fam96a forms stable monomers and dimers in solution. Crystal structures of these two forms revealed that each adopts a distinct type of domain-swapped dimer, one of which is stabilized by zinc binding. Two hinge loops control Fam96a domain swapping; both are flexible and highly conserved, suggesting that domain swapping may be a common feature of eukaryotic but not bacterial DUF59 proteins. The derived monomer fold of Fam96a diverges from that of bacterial DUF59 counterparts in that the C-terminal region of Fam96a is much longer and is positioned on the opposite side of the N-terminal core fold. The putative metal-binding site of bacterial DUF59 proteins is not conserved in Fam96a, but Fam96a interacts tightly in vitro with Ciao1, the cytosolic iron-assembly protein. Moreover, Fam96a and Ciao1 can be co-immunoprecipitated, suggesting that the interaction also occurs in vivo. Although predicted to have a signal peptide, it is shown that Fam96a is cytoplasmic. The data reveal that eukaryotic DUF59 proteins share intriguing characteristics with amyloidogenic proteins.
Keyword Macrophages
Domain swapping
Protein-protein interactions
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
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Created: Thu, 28 Jun 2012, 11:33:32 EST by Lucy O'Brien on behalf of School of Chemistry & Molecular Biosciences