6l4a: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The ~~entry 6l4a~~ is ~~ON HOLD~~

==H3-H3-H3 tri-nucleosome with the 22 base-pair linker DNA==

== Structural highlights ==

<table><tr><td colspan='2'>[[6l4a]] is a 26 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L4A FirstGlance]. <br>

</td></tr><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=6l4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l4a OCA], [http://pdbe.org/6l4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l4a RCSB], [http://www.ebi.ac.uk/pdbsum/6l4a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l4a ProSAT]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] 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.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>

== Publication Abstract from PubMed ==

The histone H3 variant CENP-A is a crucial epigenetic marker for centromere specification. CENP-A forms a characteristic nucleosome and dictates the higher-order configuration of centromeric chromatin. However, little is known about how the CENP-A nucleosome affects the architecture of centromeric chromatin. In this study, we reconstituted tri-nucleosomes mimicking a centromeric nucleosome arrangement containing the CENP-A nucleosome, and determined their 3D structures by cryoelectron microscopy. The H3-CENP-A-H3 tri-nucleosomes adopt an untwisted architecture, with an outward-facing linker DNA path between nucleosomes. This is distinct from the H3-H3-H3 tri-nucleosome architecture, with an inward-facing DNA path. Intriguingly, the untwisted architecture may allow the CENP-A nucleosome to be exposed to the solvent in the condensed chromatin model. These results provide a structural basis for understanding the 3D configuration of CENP-A-containing chromatin, and may explain how centromeric proteins can specifically target the CENP-A nucleosomes buried in robust amounts of H3 nucleosomes in centromeres.

~~Authors~~:

Cryo-EM Structures of Centromeric Tri-nucleosomes Containing a Central CENP-A Nucleosome.,Takizawa Y, Ho CH, Tachiwana H, Matsunami H, Kobayashi W, Suzuki M, Arimura Y, Hori T, Fukagawa T, Ohi MD, Wolf M, Kurumizaka H Structure. 2019 Nov 7. pii: S0969-2126(19)30357-0. doi:, 10.1016/j.str.2019.10.016. PMID:31711756<ref>PMID:31711756</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Ho, C H]]

[[Category: Kurumizaka, H]]

[[Category: Matsunami, H]]

[[Category: Ohi, M]]

[[Category: Tachiwana, H]]

[[Category: Takizawa, Y]]

[[Category: Wolf, M]]

[[Category: Centromere]]

[[Category: Chromatin]]

[[Category: Nuclear protein]]

[[Category: Nucleosome]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6l4a is ON HOLD
+==H3-H3-H3 tri-nucleosome with the 22 base-pair linker DNA==
+<StructureSection load='6l4a' size='340' side='right'caption='[[6l4a]], [[Resolution|resolution]] 12.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6l4a]] is a 26 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L4A FirstGlance]. <br>
+</td></tr><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=6l4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l4a OCA], [http://pdbe.org/6l4a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l4a RCSB], [http://www.ebi.ac.uk/pdbsum/6l4a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l4a ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] 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.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>   Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The histone H3 variant CENP-A is a crucial epigenetic marker for centromere specification. CENP-A forms a characteristic nucleosome and dictates the higher-order configuration of centromeric chromatin. However, little is known about how the CENP-A nucleosome affects the architecture of centromeric chromatin. In this study, we reconstituted tri-nucleosomes mimicking a centromeric nucleosome arrangement containing the CENP-A nucleosome, and determined their 3D structures by cryoelectron microscopy. The H3-CENP-A-H3 tri-nucleosomes adopt an untwisted architecture, with an outward-facing linker DNA path between nucleosomes. This is distinct from the H3-H3-H3 tri-nucleosome architecture, with an inward-facing DNA path. Intriguingly, the untwisted architecture may allow the CENP-A nucleosome to be exposed to the solvent in the condensed chromatin model. These results provide a structural basis for understanding the 3D configuration of CENP-A-containing chromatin, and may explain how centromeric proteins can specifically target the CENP-A nucleosomes buried in robust amounts of H3 nucleosomes in centromeres.
-Authors:
+Cryo-EM Structures of Centromeric Tri-nucleosomes Containing a Central CENP-A Nucleosome.,Takizawa Y, Ho CH, Tachiwana H, Matsunami H, Kobayashi W, Suzuki M, Arimura Y, Hori T, Fukagawa T, Ohi MD, Wolf M, Kurumizaka H Structure. 2019 Nov 7. pii: S0969-2126(19)30357-0. doi:, 10.1016/j.str.2019.10.016. PMID:31711756<ref>PMID:31711756</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6l4a" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Ho, C H]]
+[[Category: Kurumizaka, H]]
+[[Category: Matsunami, H]]
+[[Category: Ohi, M]]
+[[Category: Tachiwana, H]]
+[[Category: Takizawa, Y]]
+[[Category: Wolf, M]]
+[[Category: Centromere]]
+[[Category: Chromatin]]
+[[Category: Nuclear protein]]
+[[Category: Nucleosome]]