7w5m: Difference between revisions
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==Crystal structure of AtNASP in complex of H3 alpha3 helix peptide== | |||
<StructureSection load='7w5m' size='340' side='right'caption='[[7w5m]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7w5m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W5M 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]] 2.15Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7w5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w5m OCA], [https://pdbe.org/7w5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w5m RCSB], [https://www.ebi.ac.uk/pdbsum/7w5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w5m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q94K88_ARATH Q94K88_ARATH] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structural basis for histone recognition by the histone chaperone nuclear autoantigenic sperm protein (NASP) remains largely unclear. Here, we showed that Arabidopsis thaliana AtNASP is a monomer and displays robust nucleosome assembly activity in vitro. Examining the structure of AtNASP complexed with a histone H3 alpha3 peptide revealed a binding mode that is conserved in human NASP. AtNASP recognizes the H3 N-terminal region distinct from human NASP. Moreover, AtNASP forms a co-chaperone complex with ANTI-SILENCING FUNCTION 1 (ASF1) by binding to the H3 N-terminal region. Therefore, we deciphered the structure of AtNASP and the basis of the AtNASP-H3 interaction. | |||
Structural basis for histone H3 recognition by NASP in Arabidopsis.,Liu Y, Chen L, Wang N, Wu B, Bao H, Huang H J Integr Plant Biol. 2022 Dec;64(12):2309-2313. doi: 10.1111/jipb.13277. Epub , 2022 Jun 13. PMID:35587028<ref>PMID:35587028</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bao | <div class="pdbe-citations 7w5m" style="background-color:#fffaf0;"></div> | ||
[[Category: Liu | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bao H]] | |||
[[Category: Liu Y]] | |||
Latest revision as of 17:36, 29 November 2023
Crystal structure of AtNASP in complex of H3 alpha3 helix peptide
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