5h67 - Revision history

OCA at 07:24, 9 August 2023

OCA — Wed, 09 Aug 2023 07:24:49 GMT

←Older revision		Revision as of 07:24, 9 August 2023
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	<StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution\|resolution]] 2.07Å' scene=''>		<StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution\|resolution]] 2.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Bacsu Bacsu~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5H67 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H67 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.072035Å</td></tr>
-	~~<tr~~ id~~='related'><td class~~="~~sblockLbl~~">~~<b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h66\|5h66]]~~, [[~~5h68~~\|~~5h68]], [[5h69\|5h69]], [[3w6j\|3w6j]], [[3w6k\|3w6k~~]]</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~smc, ylqA, BSU15940 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=5~~&id=224308 BACSU]), scpA, ypuG, BSU23220 ([http:~~/~~/www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])~~</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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [https://pdbe.org/5h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [https://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [~~http~~://pdbe.org/5h67 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU]] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> [[http://www.uniprot.org/uniprot/SCPA_BACSU SCPA_BACSU]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.[HAMAP-Rule:MF_01805]	+	[https://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacsu~~]]	+	[[Category: Bacillus subtilis subsp. subtilis str. 168]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hirano, T]]	+	[[Category: Hirano T]]
-	[[Category: Kamada, K]]	+	[[Category: Kamada K]]
-	~~[[Category: Dna binding protein-cell cycle complex]]~~	+
-	~~[[Category: Smc protein~~]]	+

OCA at 10:12, 26 February 2020

OCA — Wed, 26 Feb 2020 10:12:48 GMT

←Older revision		Revision as of 10:12, 26 February 2020
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	==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain and soaked ATP==		==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain and soaked ATP==
-	<StructureSection load='5h67' size='340' side='right' caption='[[5h67]], [[Resolution\|resolution]] 2.07Å' scene=''>	+	<StructureSection load='5h67' size='340' side='right'caption='[[5h67]], [[Resolution\|resolution]] 2.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H67 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H67 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h66\|5h66]], [[5h68\|5h68]], [[5h69\|5h69]], [[3w6j\|3w6j]], [[3w6k\|3w6k]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h66\|5h66]], [[5h68\|5h68]], [[5h69\|5h69]], [[3w6j\|3w6j]], [[3w6k\|3w6k]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">smc, ylqA, BSU15940 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), scpA, ypuG, BSU23220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [http://pdbe.org/5h67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [http://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [http://pdbe.org/5h67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [http://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacsu]]
		+	[[Category: Large Structures]]
	[[Category: Hirano, T]]		[[Category: Hirano, T]]
	[[Category: Kamada, K]]		[[Category: Kamada, K]]
	[[Category: Dna binding protein-cell cycle complex]]		[[Category: Dna binding protein-cell cycle complex]]
	[[Category: Smc protein]]		[[Category: Smc protein]]

OCA at 06:27, 19 April 2017

OCA — Wed, 19 Apr 2017 06:27:53 GMT

←Older revision		Revision as of 06:27, 19 April 2017
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	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU]] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> [[http://www.uniprot.org/uniprot/SCPA_BACSU SCPA_BACSU]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.[HAMAP-Rule:MF_01805]		[[http://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU]] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> [[http://www.uniprot.org/uniprot/SCPA_BACSU SCPA_BACSU]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.[HAMAP-Rule:MF_01805]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SMC-ScpAB complex plays a crucial role in chromosome organization and segregation in many bacteria. It is composed of a V-shaped SMC dimer and an ScpAB subcomplex that bridges the two Structural Maintenance of Chromosomes (SMC) head domains. Despite its functional significance, the mechanistic details of SMC-ScpAB remain obscure. Here we provide evidence that ATP-dependent head-head engagement induces a lever movement of the SMC neck region, which might help to separate juxtaposed coiled-coil arms. Binding of the ScpA N-terminal domain (NTD) to the SMC neck region is negatively regulated by the ScpB C-terminal domain. Mutations in the ScpA NTD compromise this regulation and profoundly affect the overall shape of the complex. The SMC hinge domain is structurally relaxed when free from coiled-coil juxtaposition. Taken together, we propose that the structural parts of SMC-ScpAB are subjected to the balance between constraint and relaxation, cooperating to modulate dynamic conformational changes of the whole complex.
		+
		+	Overall Shapes of the SMC-ScpAB Complex Are Determined by Balance between Constraint and Relaxation of Its Structural Parts.,Kamada K, Su'etsugu M, Takada H, Miyata M, Hirano T Structure. 2017 Apr 4;25(4):603-616.e4. doi: 10.1016/j.str.2017.02.008. Epub 2017, Mar 9. PMID:28286005<ref>PMID:28286005</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5h67" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 21:16, 15 March 2017

OCA — Wed, 15 Mar 2017 21:16:46 GMT

←Older revision		Revision as of 21:16, 15 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5h67 is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of the Bacillus subtilis SMC head domain complexed with the cognate ScpA C-terminal domain and soaked ATP==
-		+	<StructureSection load='5h67' size='340' side='right' caption='[[5h67]], [[Resolution\|resolution]] 2.07Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5h67]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H67 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H67 FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5h66\|5h66]], [[5h68\|5h68]], [[5h69\|5h69]], [[3w6j\|3w6j]], [[3w6k\|3w6k]]</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=5h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h67 OCA], [http://pdbe.org/5h67 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h67 RCSB], [http://www.ebi.ac.uk/pdbsum/5h67 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h67 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SMC_BACSU SMC_BACSU]] Required for chromosome condensation and partitioning.<ref>PMID:9573042</ref> <ref>PMID:9701812</ref> [[http://www.uniprot.org/uniprot/SCPA_BACSU SCPA_BACSU]] Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.[HAMAP-Rule:MF_01805]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Hirano, T]]
		+	[[Category: Kamada, K]]
		+	[[Category: Dna binding protein-cell cycle complex]]
		+	[[Category: Smc protein]]

OCA at 09:26, 9 March 2017

OCA — Thu, 09 Mar 2017 09:26:14 GMT

←Older revision		Revision as of 09:26, 9 March 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5h67 is ON HOLD	+	The entry 5h67 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5h67" [edit=sysop:move=sysop]

OCA — Fri, 09 Dec 2016 13:47:24 GMT

Protected "5h67" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:47, 9 December 2016

OCA: New page: '''Unreleased structure''' The entry 5h67 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Fri, 09 Dec 2016 13:47:23 GMT

New page: '''Unreleased structure''' The entry 5h67 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5h67 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]