9qt2: Difference between revisions
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==Bacterial histone HLp from Leptospira perolatii bound to DNA== | |||
<StructureSection load='9qt2' size='340' side='right'caption='[[9qt2]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9qt2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/DNA_molecule DNA molecule] and [https://en.wikipedia.org/wiki/Leptospira_perolatii Leptospira perolatii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QT2 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]] 1.9Å</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=9qt2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qt2 OCA], [https://pdbe.org/9qt2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qt2 RCSB], [https://www.ebi.ac.uk/pdbsum/9qt2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qt2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2M9ZN55_9LEPT A0A2M9ZN55_9LEPT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Histones are conserved DNA-packaging proteins found across all domains of life. In eukaryotes, canonical histones form octamers that wrap ~147 base pairs (bp) of DNA into nucleosomes, while in archaea they form dimers that polymerize into extended hypernucleosomes. Although bacteria were long thought to lack histones, homologs have now been identified in diverse lineages. We previously characterized the histone HBb from Bdellovibrio bacteriovorus, which binds and bends DNA as a dimer. Here, we describe HLp from Leptospira perolatii and show by crystallographic and biophysical analyses that, unlike HBb, it forms stable tetramers and binds DNA nonspecifically, wrapping ~60 bp of DNA around its core. Molecular dynamics simulations, DNA-binding assays, and heterologous expression in Escherichia coli, where HLp reorganizes the nucleoid, support a role in bacterial chromatin organization. These findings expand the repertoire of bacterial histone-DNA interactions and highlight the diversity of histone-based genome organization across the tree of life. | |||
DNA Wrapping by a tetrameric bacterial histone.,Hu Y, Schwab S, Qiu K, Zhang Y, Bar K, Reichle H, Panzera A, Lupas AN, Hartmann MD, Dame RT, Alva V, Hernandez Alvarez B Nat Commun. 2025 Dec 11;16(1):11108. doi: 10.1038/s41467-025-67425-w. PMID:41381525<ref>PMID:41381525</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9qt2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA molecule]] | |||
[[Category: Large Structures]] | |||
[[Category: Leptospira perolatii]] | |||
[[Category: Albrecht R]] | |||
[[Category: Hartmann MD]] | |||
[[Category: Hu Y]] | |||
Latest revision as of 05:25, 24 December 2025
Bacterial histone HLp from Leptospira perolatii bound to DNA
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