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5jxt

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==Crystal structure of MtISWI bound with histone H4 tail==
==Crystal structure of MtISWI bound with histone H4 tail==
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<StructureSection load='5jxt' size='340' side='right' caption='[[5jxt]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
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<StructureSection load='5jxt' size='340' side='right'caption='[[5jxt]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jxt]] is a 23 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JXT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jxt]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Saitoella_complicata_NRRL_Y-17804 Saitoella complicata NRRL Y-17804] and [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JXT FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jxr|5jxr]]</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]] 3.009&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxt OCA], [http://pdbe.org/5jxt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jxt RCSB], [http://www.ebi.ac.uk/pdbsum/5jxt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxt ProSAT]</span></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=5jxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jxt OCA], [https://pdbe.org/5jxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jxt RCSB], [https://www.ebi.ac.uk/pdbsum/5jxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jxt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A0A0E9NAT8_9ASCO A0A0E9NAT8_9ASCO]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[SAAS:SAAS00581158]
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[https://www.uniprot.org/uniprot/G2QFM3_MYCTT G2QFM3_MYCTT]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ISWI is a member of the SWI2/SNF2 family of chromatin remodellers, which also includes Snf2, Chd1, and Ino80. ISWI is the catalytic subunit of several chromatin remodelling complexes, which mobilize nucleosomes along genomic DNA, promoting replication progression, transcription repression, heterochromatin formation, and many other nuclear processes. The ATPase motor of ISWI is an autonomous remodelling machine, whereas its carboxy (C)-terminal HAND-SAND-SLIDE (HSS) domain functions in binding extranucleosomal linker DNA. The activity of the catalytic core of ISWI is inhibited by the regulatory AutoN and NegC domains, which are in turn antagonized by the H4 tail and extranucleosomal DNA, respectively, to ensure the appropriate chromatin landscape in cells. How AutoN and NegC inhibit ISWI and regulate its nucleosome-centring activity remains elusive. Here we report the crystal structures of ISWI from the thermophilic yeast Myceliophthora thermophila and its complex with a histone H4 peptide. Our data show the amino (N)-terminal AutoN domain contains two inhibitory elements, which collectively bind the second RecA-like domain (core2), holding the enzyme in an inactive conformation. The H4 peptide binds to the core2 domain coincident with one of the AutoN-binding sites, explaining the ISWI activation by H4. The H4-binding surface is conserved in Snf2 and functions beyond AutoN regulation. The C-terminal NegC domain is involved in binding to the core2 domain and functions as an allosteric element for ISWI to respond to the extranucleosomal DNA length.
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Structure and regulation of the chromatin remodeller ISWI.,Yan L, Wang L, Tian Y, Xia X, Chen Z Nature. 2016 Dec 15;540(7633):466-469. doi: 10.1038/nature20590. Epub 2016 Dec 5. PMID:27919072<ref>PMID:27919072</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 5jxt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chen, Z]]
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[[Category: Large Structures]]
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[[Category: Yan, L]]
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[[Category: Saitoella complicata NRRL Y-17804]]
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[[Category: Chromatin remodeler]]
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[[Category: Thermothelomyces thermophilus ATCC 42464]]
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[[Category: Iswi]]
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[[Category: Chen Z]]
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[[Category: Transcription]]
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[[Category: Yan L]]

Current revision

Crystal structure of MtISWI bound with histone H4 tail

PDB ID 5jxt

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