5k98 - Revision history

OCA at 13:04, 1 March 2024

2024-03-01T13:04:59Z

←Older revision		Revision as of 13:04, 1 March 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>		[https://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Multidrug tolerance is largely responsible for chronic infections and caused by a small population of dormant cells called persisters. Selection for survival in the presence of antibiotics produced the first genetic link to multidrug tolerance: a mutant in the Escherichia coli hipA locus. HipA encodes a serine-protein kinase, the multidrug tolerance activity of which is neutralized by binding to the transcriptional regulator HipB and hipBA promoter. The physiological role of HipA in multidrug tolerance, however, has been unclear. Here we show that wild-type HipA contributes to persister formation and that high-persister hipA mutants cause multidrug tolerance in urinary tract infections. Perplexingly, high-persister mutations map to the N-subdomain-1 of HipA far from its active site. Structures of higher-order HipA-HipB-promoter complexes reveal HipA forms dimers in these assemblies via N-subdomain-1 interactions that occlude their active sites. High-persistence mutations, therefore, diminish HipA-HipA dimerization, thereby unleashing HipA to effect multidrug tolerance. Thus, our studies reveal the mechanistic basis of heritable, clinically relevant antibiotic tolerance.
-
-	HipBA-promoter structures reveal the basis of heritable multidrug tolerance.,Schumacher MA, Balani P, Min J, Chinnam NB, Hansen S, Vulic M, Lewis K, Brennan RG Nature. 2015 Aug 6;524(7563):59-64. doi: 10.1038/nature14662. Epub 2015 Jul 29. PMID:26222023<ref>PMID:26222023</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5k98" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 10:43, 27 September 2023

2023-09-27T10:43:39Z

←Older revision		Revision as of 10:43, 27 September 2023
Line 3:		Line 3:
	<StructureSection load='5k98' size='340' side='right'caption='[[5k98]], [[Resolution\|resolution]] 3.99Å' scene=''>		<StructureSection load='5k98' size='340' side='right'caption='[[5k98]], [[Resolution\|resolution]] 3.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~] ~~and~~ [~~http~~://en.wikipedia.org/wiki/~~Escherichia_coli_mp020980~~.2 Escherichia coli ~~mp020980~~.2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5K98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Escherichia_coli_MP020980.2 Escherichia coli MP020980.2] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K98 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>hipA, b1507, JW1500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id~~=83333 ECOLI]), hipB, ECMP0209802_2194 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1116139 Escherichia coli MP020980.2])</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]] 3.99Å</td></tr>
-	~~<tr id='activity'><td class~~="~~sblockLbl~~">~~<b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non~~-~~specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase]~~, ~~with EC number~~ [~~http://www~~.~~brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [https://pdbe.org/5k98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [https://www.ebi.ac.uk/pdbsum/5k98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k98 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [~~http~~://pdbe.org/5k98 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5k98 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5k98 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>	+	[https://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
-	[[Category: Escherichia coli ~~mp020980~~ 2]]	+	[[Category: Escherichia coli MP020980 2]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Synthetic construct]]
-	[[Category: Schumacher, M]]	+	[[Category: Schumacher M]]
-	~~[[Category: E. coli]]~~	+
-	~~[[Category: Hipa]]~~	+
-	~~[[Category: Persistence]]~~	+
-	~~[[Category: Transcription-dna complex~~]]	+

OCA at 09:28, 1 July 2020

2020-07-01T09:28:03Z

←Older revision		Revision as of 09:28, 1 July 2020
Line 1:		Line 1:

	==Structure of HipA-HipB-O2-O3 complex==		==Structure of HipA-HipB-O2-O3 complex==
-	<StructureSection load='5k98' size='340' side='right' caption='[[5k98]], [[Resolution\|resolution]] 3.99Å' scene=''>	+	<StructureSection load='5k98' size='340' side='right'caption='[[5k98]], [[Resolution\|resolution]] 3.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5K98 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli] and [http://en.wikipedia.org/wiki/Escherichia_coli_mp020980.2 Escherichia coli mp020980.2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5K98 FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hipA, b1507, JW1500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), hipB, ECMP0209802_2194 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1116139 Escherichia coli MP020980.2])</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=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [http://pdbe.org/5k98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [http://www.ebi.ac.uk/pdbsum/5k98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k98 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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [http://pdbe.org/5k98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [http://www.ebi.ac.uk/pdbsum/5k98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k98 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5k98" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5k98" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine/threonine protein kinase 3D structures\|Serine/threonine protein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ecoli]]
		+	[[Category: Escherichia coli mp020980 2]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Schumacher, M]]		[[Category: Schumacher, M]]

OCA at 02:29, 13 July 2016

2016-07-13T02:29:03Z

←Older revision		Revision as of 02:29, 13 July 2016
Line 5:		Line 5:
	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K98 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K98 FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [http://pdbe.org/5k98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [http://www.ebi.ac.uk/pdbsum/5k98 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=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [http://pdbe.org/5k98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [http://www.ebi.ac.uk/pdbsum/5k98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k98 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 23:14, 23 June 2016

2016-06-23T23:14:30Z

←Older revision		Revision as of 23:14, 23 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5k98 is ~~ON HOLD~~ ~~until sometime~~ in the ~~future~~	+	==Structure of HipA-HipB-O2-O3 complex==
		+	<StructureSection load='5k98' size='340' side='right' caption='[[5k98]], [[Resolution\|resolution]] 3.99Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5k98]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K98 FirstGlance]. <br>
		+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=5k98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k98 OCA], [http://pdbe.org/5k98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k98 RCSB], [http://www.ebi.ac.uk/pdbsum/5k98 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HIPA_ECOLI HIPA_ECOLI]] Toxic component of a toxin-antitoxin (TA) module. Autophosphorylates (Ser-150) and phosphorylates EF-Tu in vitro (on 'Thr-383'), may act on other proteins as well. The hipA7 mutation leads to increased generation of persister cells, cells that survive antibiotic treatment probably by entering into a dormant state. Wild-type cells produce persisters at a frequency of 10-6 to 10-5 whereas mutant hipA7 cells produce persisters at a frequency of 10-2. Generation of persister cells requires (p)ppGpp as cells lacking relA or relA/spoT generate fewer or no persister cells respectively compared to hipA7. Low level expression of HipA causes cell filamentation and depending on the protein level is toxic enough to reduce cell growth or even kill cells. Expression of wild-type HipA also leads to high antibiotic tolerance of the survivor cells. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. With HipB acts as a corepressor for transcription of the hipBA promoter.<ref>PMID:17041039</ref> <ref>PMID:6348026</ref> <ref>PMID:8021189</ref> <ref>PMID:14622409</ref> <ref>PMID:19150849</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Multidrug tolerance is largely responsible for chronic infections and caused by a small population of dormant cells called persisters. Selection for survival in the presence of antibiotics produced the first genetic link to multidrug tolerance: a mutant in the Escherichia coli hipA locus. HipA encodes a serine-protein kinase, the multidrug tolerance activity of which is neutralized by binding to the transcriptional regulator HipB and hipBA promoter. The physiological role of HipA in multidrug tolerance, however, has been unclear. Here we show that wild-type HipA contributes to persister formation and that high-persister hipA mutants cause multidrug tolerance in urinary tract infections. Perplexingly, high-persister mutations map to the N-subdomain-1 of HipA far from its active site. Structures of higher-order HipA-HipB-promoter complexes reveal HipA forms dimers in these assemblies via N-subdomain-1 interactions that occlude their active sites. High-persistence mutations, therefore, diminish HipA-HipA dimerization, thereby unleashing HipA to effect multidrug tolerance. Thus, our studies reveal the mechanistic basis of heritable, clinically relevant antibiotic tolerance.

-	~~Authors:~~ Schumacher, M.	+	HipBA-promoter structures reveal the basis of heritable multidrug tolerance.,Schumacher MA, Balani P, Min J, Chinnam NB, Hansen S, Vulic M, Lewis K, Brennan RG Nature. 2015 Aug 6;524(7563):59-64. doi: 10.1038/nature14662. Epub 2015 Jul 29. PMID:26222023<ref>PMID:26222023</ref>

-	~~Description: Structure~~ of ~~HipA~~-~~HipB~~-~~O2-O3 complex~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5k98" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Schumacher, M]]		[[Category: Schumacher, M]]
		+	[[Category: E. coli]]
		+	[[Category: Hipa]]
		+	[[Category: Persistence]]
		+	[[Category: Transcription-dna complex]]

OCA: Protected "5k98" [edit=sysop:move=sysop]

2016-06-20T13:35:22Z

Protected "5k98" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:35, 20 June 2016

OCA: New page: '''Unreleased structure''' The entry 5k98 is ON HOLD until sometime in the future Authors: Schumacher, M. Description: Structure of HipA-HipB-O2-O3 complex [[Category: Unreleased Struc...

2016-06-20T13:35:21Z

New page: '''Unreleased structure''' The entry 5k98 is ON HOLD until sometime in the future Authors: Schumacher, M. Description: Structure of HipA-HipB-O2-O3 complex [[Category: Unreleased Struc...

New page

'''Unreleased structure'''

The entry 5k98 is ON HOLD until sometime in the future

Authors: Schumacher, M.

Description: Structure of HipA-HipB-O2-O3 complex
[[Category: Unreleased Structures]]
[[Category: Schumacher, M]]