6n2g: Difference between revisions

Line 1:

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

~~The entry~~ 6n2g is ~~ON HOLD until Paper~~ Publication

==Crystal structure of Caenorhabditis elegans NAP1==

== Structural highlights ==

<table><tr><td colspan='2'>[[6n2g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N2G 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=6n2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n2g OCA], [http://pdbe.org/6n2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n2g RCSB], [http://www.ebi.ac.uk/pdbsum/6n2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n2g ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Nucleosome assembly proteins (Naps) influence chromatin dynamics by directly binding to histones. Here we provide a comprehensive structural and biochemical analysis of a Nap protein from Caenorhabditis elegans (CeNap1). CeNap1 naturally lacks the acidic N-terminal tail and has a short C-terminal tail compared to many other Nap proteins. Comparison with full length and a tail-less constructs of Saccharomyces cerevisiae Nap1 (ScNap1) uncovers the role of these tails in self-association, histone-binding, and competing H2A-H2B from DNA. We find that the presence of tails influences the stoichiometry of H2A-H2B-binding and is required to compete interactions between H2A-H2B and DNA. The absolute stoichiometry of the Nap protein and H2A-H2B complex is 2:1 or 2:2, with only a very small population of higher-order oligomers occurring at 150 mM NaCl. We also show that H3-H4 binds differently than H2A-H2B, and that a (H3-H4)2 tetramer can simultaneously bind two Nap2 protein homodimers.

~~Authors:~~ Bhattacharyya, S., ~~DArcy~~, S.

Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding.,Sarkar P, Zhang N, Bhattacharyya S, Salvador K, D'Arcy S Biochemistry. 2018 Dec 6. doi: 10.1021/acs.biochem.8b01033. PMID:30521320<ref>PMID:30521320</ref>

~~Description: Crystal structure~~ of ~~Caenorhabditis elegans NAP1~~

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

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

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Bhattacharyya, S]]

[[Category: ~~Darcy~~, S]]

[[Category: DArcy, S]]

[[Category: Chaperone]]

[[Category: Histone binding]]

[[Category: Nucleosome assembly]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6n2g is ON HOLD  until Paper Publication
+==Crystal structure of Caenorhabditis elegans NAP1==
+<StructureSection load='6n2g' size='340' side='right' caption='[[6n2g]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6n2g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N2G 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=6n2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n2g OCA], [http://pdbe.org/6n2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n2g RCSB], [http://www.ebi.ac.uk/pdbsum/6n2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n2g ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nucleosome assembly proteins (Naps) influence chromatin dynamics by directly binding to histones. Here we provide a comprehensive structural and biochemical analysis of a Nap protein from Caenorhabditis elegans (CeNap1). CeNap1 naturally lacks the acidic N-terminal tail and has a short C-terminal tail compared to many other Nap proteins. Comparison with full length and a tail-less constructs of Saccharomyces cerevisiae Nap1 (ScNap1) uncovers the role of these tails in self-association, histone-binding, and competing H2A-H2B from DNA. We find that the presence of tails influences the stoichiometry of H2A-H2B-binding and is required to compete interactions between H2A-H2B and DNA. The absolute stoichiometry of the Nap protein and H2A-H2B complex is 2:1 or 2:2, with only a very small population of higher-order oligomers occurring at 150 mM NaCl. We also show that H3-H4 binds differently than H2A-H2B, and that a (H3-H4)2 tetramer can simultaneously bind two Nap2 protein homodimers.
-Authors: Bhattacharyya, S., DArcy, S.
+Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding.,Sarkar P, Zhang N, Bhattacharyya S, Salvador K, D'Arcy S Biochemistry. 2018 Dec 6. doi: 10.1021/acs.biochem.8b01033. PMID:30521320<ref>PMID:30521320</ref>
-Description: Crystal structure of Caenorhabditis elegans NAP1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6n2g" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bhattacharyya, S]]
-[[Category: Darcy, S]]
+[[Category: DArcy, S]]
+[[Category: Chaperone]]
+[[Category: Histone binding]]
+[[Category: Nucleosome assembly]]