3UX3
Crystal Structure of Domain-Swapped Fam96a minor dimer
Summary for 3UX3
| Entry DOI | 10.2210/pdb3ux3/pdb |
| Related | 3UX2 |
| Descriptor | MIP18 family protein FAM96A, ZINC ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | immune system, duf59, 3d domain swapping, protein-protein interaction, alpha and beta protein (a+b), cytosolic iron-sulfur protein assembly 1 |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 30305.69 |
| Authors | Chen, K.-E.,Kobe, B.,Martin, J.L. (deposition date: 2011-12-03, release date: 2012-05-30, Last modification date: 2023-11-08) |
| Primary citation | Chen, K.E.,Richards, A.A.,Ariffin, J.K.,Ross, I.L.,Sweet, M.J.,Kellie, S.,Kobe, B.,Martin, J.L. The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer. Acta Crystallogr.,Sect.D, 68:637-648, 2012 Cited by PubMed 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. PubMed: 22683786DOI: 10.1107/S0907444912006592 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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