View source for 22gf


==Crystal structure of the C-terminal domain of Schizosaccharomyces pombe FKBP nucleoplasmin SpAni2==
<StructureSection load='22gf' size='340' side='right'caption='[[22gf]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22gf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22GF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22GF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.488&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=22gf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22gf OCA], [https://pdbe.org/22gf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22gf RCSB], [https://www.ebi.ac.uk/pdbsum/22gf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22gf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKBPH_SCHPO FKBPH_SCHPO] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Unravelling the structure-function features of Ani2, a dual chaperone from Schizosaccharomyces pombe.,Samal A, Patnaik P, Vasudevan D Int J Biol Macromol. 2026 Sep 15;383(Pt 1):154525. doi: , 10.1016/j.ijbiomac.2026.154525. PMID:42744269<ref>PMID:42744269</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 22gf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe]]
[[Category: Samal A]]
[[Category: Vasudevan D]]