4nq0

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4nq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NQ0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4nq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NQ0 FirstGlance]. <br>
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</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=4nq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nq0 OCA], [https://pdbe.org/4nq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4nq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nq0 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nq0 OCA], [https://pdbe.org/4nq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4nq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nq0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</ref>
[https://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</ref>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Yeast Hif1, a homologue of human nuclear autoantigenic sperm protein (NASP), is a histone chaperone that involved in various protein complexes modifying histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, here, we present crystal structure of Hif1 that consists of a superhelixed TPR domain and an extended acid loop covering the rear of TPR domain, which represents typical characters of SHNi-TPR (Sim3-Hif1-NASP interrupted TPR) proteins. Our binding assay indicates that Hif1 could bind to histone octamer via histone H3 and H4. However, the acid loop is crucial for the binding of histones while it may also change the conformation of TPR groove. By binding to core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.
 
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Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones.,Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, Niu L Biochem J. 2014 Jun 20. PMID:24946827<ref>PMID:24946827</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 4nq0" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones

PDB ID 4nq0

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