22GF

Crystal structure of the C-terminal domain of Schizosaccharomyces pombe FKBP nucleoplasmin SpAni2

Summary for 22GF

• Entry DOI: 10.2210/pdb22gf/pdb
• Descriptor: Probable peptidyl-prolyl cis-trans isomerase C27F1.06c (2 entities in total)
• Functional Keywords: fkbp, ppiase, isomerase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Total number of polymer chains: 3
• Total formula weight: 38871.48

Authors

Samal, A.,Vasudevan, D. (deposition date: 2026-01-09, release date: 2026-09-30)

Primary citation

Samal, A.,Patnaik, P.,Vasudevan, D.
Unravelling the structure-function features of Ani2, a dual chaperone from Schizosaccharomyces pombe.
Int.J.Biol.Macromol., 383:154525-154525, 2026

PubMed Abstract: Histone chaperones play significant roles in histone storage, transport, and assembly to form nucleosomes. Nucleoplasmin, a family of histone chaperones, has been reported from across the eukaryotic spectrum. Among these, the FK506-binding protein (FKBP) nucleoplasmin class, present in yeast, plants, and arthropods, possesses a nucleoplasmin core domain at the N-terminus, a central acidic stretch, and a characteristic C-terminal FKBP domain. CENP-A N-terminal domain isomerase 2 (Ani2) is an FKBP nucleoplasmin reported from the fission yeast, Schizosaccharomyces pombe. Ani2 has not been characterized in terms of its domain organization, chaperoning functions, and structural features. Herein, we undertook a domain-dissection approach and report the structural and in vitro functional attributes of Ani2. The N-terminal nucleoplasmin domain formed a pentamer, and the C-terminal domain (CTD) revealed a characteristic monomeric fold of an FKBP. The N-terminal domain (NTD) showed histone chaperone activity in vitro, and the FKBP domain functioned as a prolyl isomerase, confirming that this is a dual chaperone. Moreover, the CTD efficiently binds to the immunosuppressive compounds FK506 and rapamycin.

PubMed: 42744269
DOI: 10.1016/j.ijbiomac.2026.154525

Experimental method

X-RAY DIFFRACTION (2.488 Å)