4git - Revision history

OCA at 13:59, 8 November 2023

2023-11-08T13:59:39Z

← Older revision		Revision as of 13:59, 8 November 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.882Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [https://pdbe.org/4git PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [https://www.ebi.ac.uk/pdbsum/4git PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4git 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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [https://pdbe.org/4git PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [https://www.ebi.ac.uk/pdbsum/4git PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:58, 26 October 2022

2022-10-26T06:58:54Z

← Older revision		Revision as of 06:58, 26 October 2022
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	==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==		==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
	<StructureSection load='4git' size='340' side='right' caption='[[4git]], [[Resolution\|resolution]] 2.88Å' scene=''>		<StructureSection load='4git' size='340' side='right'caption='[[4git]], [[Resolution\|resolution]] 2.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus~~ thermoruber~~" guicciardi et al. 1968~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GIT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [https://pdbe.org/4git PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [https://www.ebi.ac.uk/pdbsum/4git PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [~~http~~://pdbe.org/4git PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4git PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]		[https://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]
	<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: ~~Bacillus~~ thermoruber ~~guicciardi et al. 1968~~]]		[[Category: Brevibacillus thermoruber]]
	[[Category: ~~Endopeptidase La~~]]		[[Category: Large Structures]]
	[[Category: Chang~~, Y Y~~]]		[[Category: Chang YY]]
	[[Category: Chen~~, Y D~~]]		[[Category: Chen YD]]
	[[Category: Hsu~~, C H]]~~		[[Category: Hsu CH]]
	~~[[Category: Dna binding]]~~
	~~[[Category: Hydrolase~~]]

OCA at 06:27, 5 August 2016

2016-08-05T06:27:39Z

← Older revision		Revision as of 06:27, 5 August 2016
Line 1:		Line 1:

	==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==		==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
	<StructureSection load='4git' size='340' side='right' caption='[[4git]], [[Resolution\|resolution]] 2.88Å' scene=''>		<StructureSection load='4git' size='340' side='right' caption='[[4git]], [[Resolution\|resolution]] 2.88Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum]</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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://pdbe.org/4git PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4git ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4git" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 23:51, 24 December 2014

2014-12-24T23:51:23Z

← Older revision		Revision as of 23:51, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus thermoruber" guicciardi et al. 1968]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GIT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus thermoruber" guicciardi et al. 1968]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum]</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=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.,Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):218-30. doi:, 10.1107/S139900471302631X. Epub 2014 Jan 17. PMID:24531457<ref>PMID:24531457</ref>		Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.,Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):218-30. doi:, 10.1107/S139900471302631X. Epub 2014 Jan 17. PMID:24531457<ref>PMID:24531457</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 22:		Line 24:
	[[Category: Bacillus thermoruber guicciardi et al. 1968]]		[[Category: Bacillus thermoruber guicciardi et al. 1968]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]
	[[Category: Chang, Y Y.]]		[[Category: Chang, Y Y]]
	[[Category: Chen, Y D.]]		[[Category: Chen, Y D]]
	[[Category: Hsu, C H.]]		[[Category: Hsu, C H]]
	[[Category: Dna binding]]		[[Category: Dna binding]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 13:25, 18 May 2014

2014-05-18T13:25:47Z

← Older revision		Revision as of 13:25, 18 May 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4git~~\| ~~PDB~~=4git \| ~~SCENE~~= }}		==Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber==
	===~~Crystal~~ structure of alpha ~~sub-domain~~ of Lon protease from Brevibacillus thermoruber~~===~~		<StructureSection load='4git' size='340' side='right' caption='[[4git]], [[Resolution\|resolution]] 2.88Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermoruber"_guicciardi_et_al._1968 "bacillus thermoruber" guicciardi et al. 1968]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GIT FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">lon ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33942 "Bacillus thermoruber" Guicciardi et al. 1968])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4git FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4git OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4git RCSB], [http://www.ebi.ac.uk/pdbsum/4git PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Lon belongs to a unique group of AAA+ proteases that bind DNA. However, the DNA-mediated regulation of Lon remains elusive. Here, the crystal structure of the alpha subdomain of the Lon protease from Brevibacillus thermoruber (Bt-Lon) is presented, together with biochemical data, and the DNA-binding mode is delineated, showing that Arg518, Arg557 and Arg566 play a crucial role in DNA binding. Electrostatic interactions contributed by arginine residues in the AAA+ module are suggested to be important to DNA binding and allosteric regulation of enzymatic activities. Intriguingly, Arg557, which directly binds DNA in the alpha subdomain, has a dual role in the negative regulation of ATPase stimulation by DNA and in the domain-domain communication in allosteric regulation of Bt-Lon by substrate. In conclusion, structural and biochemical evidence is provided to show that electrostatic interaction in the AAA+ module is important for DNA binding by Lon and allosteric regulation of its enzymatic activities by DNA and substrate.

	~~==Function==~~		Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.,Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):218-30. doi:, 10.1107/S139900471302631X. Epub 2014 Jan 17. PMID:24531457<ref>PMID:24531457</ref>
	~~[[http://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] ATP~~-~~dependent serine protease that mediates~~ the ~~selective degradation~~ of ~~mutant and abnormal proteins as well as certain short~~-~~lived regulatory proteins~~. ~~Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress~~. ~~Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long~~. ~~Binds to DNA in a double-stranded, site-specific manner (By similarity)~~.~~[HAMAP-Rule~~:~~MF_01973]~~

	==~~About this Structure~~==		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
	~~[[4git]] is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA].~~		</div>
	[[Category: ~~Brevibacillus~~ thermoruber]]		== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Bacillus thermoruber guicciardi et al. 1968]]
	[[Category: Endopeptidase La]]		[[Category: Endopeptidase La]]
	[[Category: Chang, Y Y.]]		[[Category: Chang, Y Y.]]

OCA at 05:29, 12 September 2013

2013-09-12T05:29:46Z

← Older revision		Revision as of 05:29, 12 September 2013
Line 1:		Line 1:
	~~'''Unreleased~~ structure~~'''~~		{{STRUCTURE_4git\| PDB=4git \| SCENE= }}
			===Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber===

	~~The entry 4git is ON HOLD until Paper Publication~~		==Function==
			[[http://www.uniprot.org/uniprot/Q84FG5_9BACL Q84FG5_9BACL]] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner (By similarity).[HAMAP-Rule:MF_01973]

	~~Authors~~: ~~Chen, Y~~.D., Chang, Y.Y., Hsu, C.H.		==About this Structure==
			[[4git]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brevibacillus_thermoruber Brevibacillus thermoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GIT OCA].
	~~Description~~: ~~Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber~~		[[Category: Brevibacillus thermoruber]]
			[[Category: Endopeptidase La]]
			[[Category: Chang, Y Y.]]
			[[Category: Chen, Y D.]]
			[[Category: Hsu, C H.]]
			[[Category: Dna binding]]
			[[Category: Hydrolase]]

OCA at 08:34, 31 October 2012

2012-10-31T08:34:27Z

← Older revision		Revision as of 08:34, 31 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4git is ON HOLD		The entry 4git is ON HOLD until Paper Publication

	Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H.		Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H.

	Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber		Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber

OCA: Protected "4git" [edit=sysop:move=sysop]

2012-08-15T05:27:56Z

Protected "4git" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:27, 15 August 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4git is ON HOLD Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H. Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus t...

2012-08-15T05:27:55Z

New page: '''Unreleased structure''' The entry 4git is ON HOLD Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H. Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus t...

New page

'''Unreleased structure'''

The entry 4git is ON HOLD

Authors: Chen, Y.D., Chang, Y.Y., Hsu, C.H.

Description: Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber