8cmp - Revision history

OCA at 09:47, 9 October 2024

2024-10-09T09:47:32Z

← Older revision		Revision as of 09:47, 9 October 2024
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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=8cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cmp OCA], [https://pdbe.org/8cmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cmp RCSB], [https://www.ebi.ac.uk/pdbsum/8cmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cmp ProSAT]</span></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=8cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cmp OCA], [https://pdbe.org/8cmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cmp RCSB], [https://www.ebi.ac.uk/pdbsum/8cmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cmp ProSAT]</span></td></tr>
	</table>		</table>
	== ~~Function~~ ==		<div style="background-color:#fffaf0;">
	~~[https~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~A0A150WQJ8_BDEBC A0A150WQJ8_BDEBC]~~		== Publication Abstract from PubMed ==
			Histones are essential for genome compaction and transcription regulation in eukaryotes, where they assemble into octamers to form the nucleosome core. In contrast, archaeal histones assemble into dimers that form hypernucleosomes upon DNA binding. Although histone homologs have been identified in bacteria recently, their DNA-binding characteristics remain largely unexplored. Our study reveals that the bacterial histone HBb (Bd0055) is indispensable for the survival of Bdellovibrio bacteriovorus, suggesting critical roles in DNA organization and gene regulation. By determining crystal structures of free and DNA-bound HBb, we unveil its distinctive dimeric assembly, diverging from those of eukaryotic and archaeal histones, while also elucidating how it binds and bends DNA through interaction interfaces reminiscent of eukaryotic and archaeal histones. Building on this, by employing various biophysical and biochemical approaches, we further substantiated the ability of HBb to bind and compact DNA by bending in a sequence-independent manner. Finally, using DNA affinity purification and sequencing, we reveal that HBb binds along the entire genomic DNA of B. bacteriovorus without sequence specificity. These distinct DNA-binding properties of bacterial histones, showcasing remarkable similarities yet significant differences from their archaeal and eukaryotic counterparts, highlight the diverse roles histones play in DNA organization across all domains of life.

			Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending.,Hu Y, Schwab S, Deiss S, Escudeiro P, van Heesch T, Joiner JD, Vreede J, Hartmann MD, Lupas AN, Alvarez BH, Alva V, Dame RT Nucleic Acids Res. 2024 Jun 12:gkae485. doi: 10.1093/nar/gkae485. PMID:38864377<ref>PMID:38864377</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 8cmp" style="background-color:#fffaf0;"></div>
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:02, 6 March 2024

2024-03-06T12:02:14Z

← Older revision		Revision as of 12:02, 6 March 2024
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	~~'''Unreleased structure'''~~

	~~The entry~~ 8cmp is ~~ON HOLD until Paper Publication~~		==DNA-binding bacterial histone protein HBB from Bdellovibrio bacteriovorus==
			<StructureSection load='8cmp' size='340' side='right'caption='[[8cmp]], [[Resolution\|resolution]] 1.06Å' scene=''>
	~~Authors~~:		== Structural highlights ==
			<table><tr><td colspan='2'>[[8cmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus Bdellovibrio bacteriovorus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CMP FirstGlance]. <br>
	~~Description~~:		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.06Å</td></tr>
	[[Category: ~~Unreleased~~ Structures]]		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8cmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cmp OCA], [https://pdbe.org/8cmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cmp RCSB], [https://www.ebi.ac.uk/pdbsum/8cmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cmp ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/A0A150WQJ8_BDEBC A0A150WQJ8_BDEBC]
			__TOC__
			</StructureSection>
			[[Category: Bdellovibrio bacteriovorus]]
			[[Category: Large Structures]]
			[[Category: Albrecht R]]
			[[Category: Hartmann MD]]
			[[Category: Hu Y]]
			[[Category: Joiner JD]]

OCA at 07:29, 15 March 2023

2023-03-15T07:29:52Z

← Older revision		Revision as of 07:29, 15 March 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8cmp is ON HOLD		The entry 8cmp is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8cmp" [edit=sysop:move=sysop]

2023-03-02T04:21:31Z

Protected "8cmp" [edit=sysop:move=sysop]

← Older revision	Revision as of 04:21, 2 March 2023
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8cmp is ON HOLD Authors: Description: Category: Unreleased Structures

2023-03-02T04:21:30Z

New page: '''Unreleased structure''' The entry 8cmp is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8cmp is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]