2h1c - Revision history

OCA at 09:30, 14 February 2024

OCA — Wed, 14 Feb 2024 09:30:41 GMT

←Older revision		Revision as of 09:30, 14 February 2024
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	<StructureSection load='2h1c' size='340' side='right'caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2h1c' size='340' side='right'caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus~~ gonorrhoeae~~" (zopf 1885) lehmann and neumann 1896~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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]] 1.8Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [https://pdbe.org/2h1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [https://www.ebi.ac.uk/pdbsum/2h1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1c 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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [https://pdbe.org/2h1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [https://www.ebi.ac.uk/pdbsum/2h1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1]] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. [[https://www.uniprot.org/uniprot/FITA_NEIG1 FITA_NEIG1]] Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.<ref>PMID:10639460</ref>	+	[https://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h1c ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h1c ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Neisseria gonorrhoeae is a sexually transmitted pathogen that initiates infections in humans by adhering to the mucosal epithelium of the urogenital tract. The bacterium then enters the apical region of the cell and traffics across the cell to exit into the subepithelial matrix. Mutations in the fast intracellular trafficking (fitAB) locus cause the bacteria to transit a polarized epithelial monolayer more quickly than the wild-type parent and to replicate within cells at an accelerated rate. Here, we describe the crystal structure of the toxin-antitoxin heterodimer, FitAB, bound to a high affinity 36-bp DNA fragment from the fitAB promoter. FitA, the antitoxin, binds DNA through its ribbon-helix-helix motif and is tethered to FitB, the toxin, to form a heterodimer by the insertion of a four turn alpha-helix into an extensive FitB hydrophobic pocket. FitB is composed of a PIN (PilT N terminus) domain, with a central, twisted, 5-stranded parallel beta-sheet that is open on one side and flanked by five alpha-helices. FitB in the context of the FitAB complex does not display nuclease activity against tested PIN substrates. The FitAB complex points to the mechanism by which antitoxins with RHH motifs can block the activity of toxins with PIN domains. Interactions between two FitB molecules result in the formation of a tetramer of FitAB heterodimers, which binds to the 36-bp DNA fragment and provides an explanation for how FitB enhances the DNA binding affinity of FitA.
-
-	Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs.,Mattison K, Wilbur JS, So M, Brennan RG J Biol Chem. 2006 Dec 8;281(49):37942-51. Epub 2006 Sep 18. PMID:16982615<ref>PMID:16982615</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2h1c" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Brennan, R G~~]]	+	[[Category: Neisseria gonorrhoeae]]
-	[[Category: ~~Mattison, K~~]]	+	[[Category: Brennan RG]]
-	[[Category: ~~So, M~~]]	+	[[Category: Mattison K]]
-	[[Category: ~~Wilbur, J S~~]]	+	[[Category: So M]]
-	[[Category: ~~Dna binding]]~~	+	[[Category: Wilbur JS]]
-	~~[[Category: Gene regulation]]~~	+
-	~~[[Category: Pin domain]]~~	+
-	~~[[Category: Rhh domain~~]]	+

OCA at 07:28, 17 March 2021

OCA — Wed, 17 Mar 2021 07:28:45 GMT

←Older revision		Revision as of 07:28, 17 March 2021
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	==Crystal Structure of FitAcB from Neisseria gonorrhoeae==		==Crystal Structure of FitAcB from Neisseria gonorrhoeae==
-	<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='2h1c' size='340' side='right'caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2H1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1C FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [~~http~~://pdbe.org/2h1c PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2h1c PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1c 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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [https://pdbe.org/2h1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [https://www.ebi.ac.uk/pdbsum/2h1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1]] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. [[~~http~~://www.uniprot.org/uniprot/FITA_NEIG1 FITA_NEIG1]] Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.<ref>PMID:10639460</ref>	+	[[https://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1]] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. [[https://www.uniprot.org/uniprot/FITA_NEIG1 FITA_NEIG1]] Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.<ref>PMID:10639460</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Brennan, R G]]		[[Category: Brennan, R G]]
	[[Category: Mattison, K]]		[[Category: Mattison, K]]

OCA at 06:32, 27 June 2018

OCA — Wed, 27 Jun 2018 06:32:15 GMT

←Older revision		Revision as of 06:32, 27 June 2018
Line 1:		Line 1:
		+
	==Crystal Structure of FitAcB from Neisseria gonorrhoeae==		==Crystal Structure of FitAcB from Neisseria gonorrhoeae==
	<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://pdbe.org/2h1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c 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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://pdbe.org/2h1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1c ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/2h1c_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/2h1c_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h1c ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:43, 12 September 2015

OCA — Sat, 12 Sep 2015 00:43:44 GMT

←Older revision		Revision as of 00:43, 12 September 2015
Line 2:		Line 2:
	<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Neisseria_gonorrhoeae Neisseria~~ gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1C FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1C FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 ~~Neisseria~~ gonorrhoeae]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 ~~Neisseria~~ gonorrhoeae])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 "Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896])</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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c 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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://pdbe.org/2h1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FITB_NEIG1 FITB_NEIG1]] Toxic component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. FitAB binds to its own promoter better than FitA alone. The expected nuclease activity was not observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB. [[http://www.uniprot.org/uniprot/FITA_NEIG1 FITA_NEIG1]] Antitoxin component of a toxin-antitoxin (TA) module. Plays a role in the speed with which bacteria traverse human epithelial cells; disruption of the locus increases the speed of trafficking about 2-4-fold. Binds to its own promoter, binding affinity of the FitAB complex is 20-30-fold higher than FitA alone. No nuclease activity was observed for the FitAB complex, perhaps because FitA (the antitoxin) prevents metal binding and thus catalysis by FitB.<ref>PMID:10639460</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 25:		Line 27:
	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 2h1c" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Neisseria gonorrhoeae]]
	[[Category: Brennan, R G]]		[[Category: Brennan, R G]]
	[[Category: Mattison, K]]		[[Category: Mattison, K]]

OCA at 09:08, 16 January 2015

OCA — Fri, 16 Jan 2015 09:08:50 GMT

←Older revision		Revision as of 09:08, 16 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1C FirstGlance]. <br>		<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1C FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae])</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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c 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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Neisseria gonorrhoeae]]		[[Category: Neisseria gonorrhoeae]]
-	[[Category: Brennan, R G.]]	+	[[Category: Brennan, R G]]
-	[[Category: Mattison, K.]]	+	[[Category: Mattison, K]]
-	[[Category: So, M.]]	+	[[Category: So, M]]
-	[[Category: Wilbur, J S.]]	+	[[Category: Wilbur, J S]]
	[[Category: Dna binding]]		[[Category: Dna binding]]
	[[Category: Gene regulation]]		[[Category: Gene regulation]]
	[[Category: Pin domain]]		[[Category: Pin domain]]
	[[Category: Rhh domain]]		[[Category: Rhh domain]]

OCA at 08:45, 30 September 2014

OCA — Tue, 30 Sep 2014 08:45:13 GMT

←Older revision		Revision as of 08:45, 30 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2h1c.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of FitAcB from Neisseria gonorrhoeae==
		+	<StructureSection load='2h1c' size='340' side='right' caption='[[2h1c]], [[Resolution\|resolution]] 1.80Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H1C FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">fitB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae]), fitA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=485 Neisseria gonorrhoeae])</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=2h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h1c RCSB], [http://www.ebi.ac.uk/pdbsum/2h1c PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/2h1c_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Neisseria gonorrhoeae is a sexually transmitted pathogen that initiates infections in humans by adhering to the mucosal epithelium of the urogenital tract. The bacterium then enters the apical region of the cell and traffics across the cell to exit into the subepithelial matrix. Mutations in the fast intracellular trafficking (fitAB) locus cause the bacteria to transit a polarized epithelial monolayer more quickly than the wild-type parent and to replicate within cells at an accelerated rate. Here, we describe the crystal structure of the toxin-antitoxin heterodimer, FitAB, bound to a high affinity 36-bp DNA fragment from the fitAB promoter. FitA, the antitoxin, binds DNA through its ribbon-helix-helix motif and is tethered to FitB, the toxin, to form a heterodimer by the insertion of a four turn alpha-helix into an extensive FitB hydrophobic pocket. FitB is composed of a PIN (PilT N terminus) domain, with a central, twisted, 5-stranded parallel beta-sheet that is open on one side and flanked by five alpha-helices. FitB in the context of the FitAB complex does not display nuclease activity against tested PIN substrates. The FitAB complex points to the mechanism by which antitoxins with RHH motifs can block the activity of toxins with PIN domains. Interactions between two FitB molecules result in the formation of a tetramer of FitAB heterodimers, which binds to the 36-bp DNA fragment and provides an explanation for how FitB enhances the DNA binding affinity of FitA.

-	~~{{STRUCTURE_2h1c\| PDB=2h1c \| SCENE= }}~~	+	Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs.,Mattison K, Wilbur JS, So M, Brennan RG J Biol Chem. 2006 Dec 8;281(49):37942-51. Epub 2006 Sep 18. PMID:16982615<ref>PMID:16982615</ref>

-	~~===Crystal Structure~~ of ~~FitAcB from Neisseria gonorrhoeae===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16982615}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2h1c]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016982615<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Neisseria gonorrhoeae]]		[[Category: Neisseria gonorrhoeae]]
	[[Category: Brennan, R G.]]		[[Category: Brennan, R G.]]

OCA: Protected "2h1c" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 13:43:11 GMT

Protected "2h1c" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:43, 7 January 2013

OCA at 13:43, 7 January 2013

OCA — Mon, 07 Jan 2013 13:43:07 GMT

←Older revision		Revision as of 13:43, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2h1c.png\|left\|200px]]		[[Image:2h1c.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2h1c", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_2h1c\| PDB=2h1c \| SCENE= }}		{{STRUCTURE_2h1c\| PDB=2h1c \| SCENE= }}

	===Crystal Structure of FitAcB from Neisseria gonorrhoeae===		===Crystal Structure of FitAcB from Neisseria gonorrhoeae===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16982615}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16982615 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16982615}}		{{ABSTRACT_PUBMED_16982615}}

	==About this Structure==		==About this Structure==
-	~~2H1C~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA].	+	[[2h1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16982615~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016982615</ref><references group="xtra"/>
	[[Category: Neisseria gonorrhoeae]]		[[Category: Neisseria gonorrhoeae]]
	[[Category: Brennan, R G.]]		[[Category: Brennan, R G.]]
Line 33:		Line 21:
	[[Category: Pin domain]]		[[Category: Pin domain]]
	[[Category: Rhh domain]]		[[Category: Rhh domain]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:28:18 2009''

OCA at 06:28, 18 February 2009

OCA — Wed, 18 Feb 2009 06:28:19 GMT

←Older revision		Revision as of 06:28, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
-	2H1C is a ~~[[Protein complex]]~~ structure of sequences from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA].	+	2H1C is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1C OCA].

	==Reference==		==Reference==
-	Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs., Mattison K, Wilbur JS, So M, Brennan RG, J Biol Chem. 2006 Dec 8;281(49):37942-51. Epub 2006 Sep 18. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16982615 16982615]~~	+	<ref group="xtra">PMID:16982615</ref><references group="xtra"/>
	[[Category: Neisseria gonorrhoeae]]		[[Category: Neisseria gonorrhoeae]]
-	[[Category: Protein complex]]
	[[Category: Brennan, R G.]]		[[Category: Brennan, R G.]]
	[[Category: Mattison, K.]]		[[Category: Mattison, K.]]
Line 35:		Line 34:
	[[Category: Rhh domain]]		[[Category: Rhh domain]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 14~~:46:~~11 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:28:18 2009''

OCA at 11:46, 29 July 2008

OCA — Tue, 29 Jul 2008 11:46:13 GMT

←Older revision		Revision as of 11:46, 29 July 2008
Line 1:		Line 1:
-	[[Image:2h1c.~~gif~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:2h1c.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_2h1c\| PDB=2h1c \| SCENE= }}		{{STRUCTURE_2h1c\| PDB=2h1c \| SCENE= }}

-	~~'''~~Crystal Structure of FitAcB from Neisseria gonorrhoeae~~'''~~	+	===Crystal Structure of FitAcB from Neisseria gonorrhoeae===


-	~~==Overview==~~	+	<!--
-	~~Neisseria gonorrhoeae is a sexually transmitted pathogen that initiates infections in humans by adhering to the mucosal epithelium of the urogenital tract.~~ The ~~bacterium then enters~~ the ~~apical region of the cell and traffics across the cell~~ to ~~exit into~~ the ~~subepithelial matrix. Mutations in the fast intracellular trafficking~~ (~~fitAB) locus cause the bacteria to transit a polarized epithelial monolayer more quickly than the wild-type parent and to replicate within cells~~ at ~~an accelerated rate~~. ~~Here, we describe the crystal structure of the toxin-antitoxin heterodimer, FitAB, bound to a high affinity 36-bp DNA fragment from the fitAB promoter~~. ~~FitA~~, ~~the antitoxin, binds DNA through its ribbon-helix-helix motif and~~ is ~~tethered to FitB,~~ the ~~toxin, to form a heterodimer by the insertion of a four turn alpha-helix into an extensive FitB hydrophobic pocket~~. ~~FitB is composed of a PIN (PilT N terminus) domain, with a central, twisted, 5~~-~~stranded parallel beta~~-sheet that is open on one side and flanked by five alpha-helices. FitB in the context of the FitAB complex does not display nuclease activity against tested PIN substrates. The FitAB complex points to the mechanism by which antitoxins with RHH motifs can block the activity of toxins with PIN domains. Interactions between two FitB molecules result in the formation of a tetramer of FitAB heterodimers, which binds to the 36-bp DNA fragment and provides an explanation for how FitB enhances the DNA binding affinity of FitA.	+	The line below this paragraph, {{ABSTRACT_PUBMED_16982615}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 16982615 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_16982615}}

	==About this Structure==		==About this Structure==
Line 30:		Line 34:
	[[Category: Pin domain]]		[[Category: Pin domain]]
	[[Category: Rhh domain]]		[[Category: Rhh domain]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 05~~:45:12 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:46:11 2008''