3UX3

Crystal Structure of Domain-Swapped Fam96a minor dimer

3UX3 の概要

• エントリーDOI: 10.2210/pdb3ux3/pdb
• 関連するPDBエントリー: 3UX2
• 分子名称: MIP18 family protein FAM96A, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: immune system, duf59, 3d domain swapping, protein-protein interaction, alpha and beta protein (a+b), cytosolic iron-sulfur protein assembly 1
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30305.69

構造登録者

Chen, K.-E.,Kobe, B.,Martin, J.L. (登録日: 2011-12-03, 公開日: 2012-05-30, 最終更新日: 2023-11-08)

主引用文献

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

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: 22683786
DOI: 10.1107/S0907444912006592

実験手法

X-RAY DIFFRACTION (1.8 Å)