View source for 7wim


==Crystal structure of Arabidopsis thaliana FKBP43 N-terminal domain==
<StructureSection load='7wim' size='340' side='right'caption='[[7wim]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wim]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WIM 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]] 2.29&#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=7wim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wim OCA], [https://pdbe.org/7wim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wim RCSB], [https://www.ebi.ac.uk/pdbsum/7wim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wim ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKB43_ARATH FKB43_ARATH] 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 ==
The nucleoplasmin family of histone chaperones is a key player in governing the dynamic architecture of chromatin, thereby regulating various DNA-templated processes. The crystal structure of the N-terminal domain of Arabidopsis thaliana FKBP43 (AtFKBP43), an FK506-binding immunophilin protein, revealed a characteristic nucleoplasmin fold, thus confirming it to be a member of the FKBP nucleoplasmin class. Small-Angle X-ray Scattering (SAXS) analyses confirmed its pentameric nature in solution, and additional studies confirmed the nucleoplasmin fold to be highly stable. Unlike its homolog AtFKBP53, the AtFKBP43 nucleoplasmin core domain could not interact with histones and required the acidic arms, C-terminal to the core, for histone association. However, SAXS generated low-resolution envelope structure, ITC, and AUC results revealed that an AtFKBP43 pentamer with C-terminal extensions interacts with H2A/H2B dimer and H3/H4 tetramer in an equimolar ratio, like AtFKBP53. Put together, AtFKBP43 belongs to a hitherto unreported subclass of FKBP nucleoplasmins that requires the C-terminal acidic stretches emanating from the core domain for histone interaction.

The plant nucleoplasmin AtFKBP43 needs its extended arms for histone interaction.,Singh AK, Saharan K, Baral S, Vasudevan D Biochim Biophys Acta Gene Regul Mech. 2022 Sep 2;1865(7):194872. doi:, 10.1016/j.bbagrm.2022.194872. PMID:36058470<ref>PMID:36058470</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wim" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Baral S]]
[[Category: Saharan K]]
[[Category: Singh AK]]
[[Category: Vasudevan D]]