4c3t - Revision history

OCA at 12:03, 20 December 2023

OCA — Wed, 20 Dec 2023 12:03:00 GMT

←Older revision		Revision as of 12:03, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3T FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.69Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [https://pdbe.org/4c3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [https://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t 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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [https://pdbe.org/4c3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [https://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/E8T502_THEA1 E8T502_THEA1]]	+	[https://www.uniprot.org/uniprot/E8T502_THEA1 E8T502_THEA1]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans alpha-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of the E. coli host cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70 degrees C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized alpha-carbonic anhydrases, TaCA does not display esterase activity towards p-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.
		+
		+	The structure of a tetrameric alpha-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability.,James P, Isupov MN, Sayer C, Saneei V, Berg S, Lioliou M, Kotlar HK, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2607-18. doi:, 10.1107/S1399004714016526. Epub 2014 Sep 27. PMID:25286845<ref>PMID:25286845</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c3t" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]		*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:24, 7 September 2022

OCA — Wed, 07 Sep 2022 17:24:38 GMT

←Older revision		Revision as of 17:24, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c3t' size='340' side='right'caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>		<StructureSection load='4c3t' size='340' side='right'caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C3T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [https://pdbe.org/4c3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [https://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t 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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [~~http~~://pdbe.org/4c3t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/E8T502_THEA1 E8T502_THEA1]]
-	Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans alpha-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of the E. coli host cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70 degrees C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized alpha-carbonic anhydrases, TaCA does not display esterase activity towards p-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.	+
-		+
-	The structure of a tetrameric alpha-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability.,James P, Isupov MN, Sayer C, Saneei V, Berg S, Lioliou M, Kotlar HK, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):~~2607-18. doi:, 10.1107~~/~~S1399004714016526. Epub 2014 Sep 27. PMID:25286845<ref>PMID:25286845<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 4c3t" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
-	*[[Carbonic anhydrase\|Carbonic anhydrase]]	+	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Carbonate dehydratase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Thermovibrio ammonificans]]		[[Category: Thermovibrio ammonificans]]
-	[[Category: Berg, S]]	+	[[Category: Berg S]]
-	[[Category: Isupov, M]]	+	[[Category: Isupov M]]
-	[[Category: James, P]]	+	[[Category: James P]]
-	[[Category: Kotlar, H]]	+	[[Category: Kotlar H]]
-	[[Category: Lioliou, M]]	+	[[Category: Lioliou M]]
-	[[Category: Littlechild, J]]	+	[[Category: Littlechild J]]
-	[[Category: Sayer, C]]	+	[[Category: Sayer C]]
-	~~[[Category: Acetazolamide]]~~	+
-	~~[[Category: Carbon dioxide capture]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Thermal stability]]~~	+
-	~~[[Category: Thermophilic~~]]	+

OCA at 09:44, 20 March 2019

OCA — Wed, 20 Mar 2019 09:44:21 GMT

←Older revision		Revision as of 09:44, 20 March 2019
Line 1:		Line 1:

	==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme==		==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme==
-	<StructureSection load='4c3t' size='340' side='right' caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>	+	<StructureSection load='4c3t' size='340' side='right'caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
		+	[[Category: Large Structures]]
	[[Category: Thermovibrio ammonificans]]		[[Category: Thermovibrio ammonificans]]
	[[Category: Berg, S]]		[[Category: Berg, S]]

OCA at 15:41, 11 August 2016

OCA — Thu, 11 Aug 2016 15:41:53 GMT

←Older revision		Revision as of 15:41, 11 August 2016
Line 1:		Line 1:
		+
	==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme==		==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme==
	<StructureSection load='4c3t' size='340' side='right' caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>		<StructureSection load='4c3t' size='340' side='right' caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t 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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://pdbe.org/4c3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3t ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4c3t" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:11, 25 January 2015

OCA — Sun, 25 Jan 2015 08:11:42 GMT

←Older revision		Revision as of 08:11, 25 January 2015
Line 21:		Line 21:
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Thermovibrio ammonificans]]		[[Category: Thermovibrio ammonificans]]
-	[[Category: Berg, S.]]	+	[[Category: Berg, S]]
-	[[Category: Isupov, M.]]	+	[[Category: Isupov, M]]
-	[[Category: James, P.]]	+	[[Category: James, P]]
-	[[Category: Kotlar, H.]]	+	[[Category: Kotlar, H]]
-	[[Category: Lioliou, M.]]	+	[[Category: Lioliou, M]]
-	[[Category: Littlechild, J.]]	+	[[Category: Littlechild, J]]
-	[[Category: Sayer, C.]]	+	[[Category: Sayer, C]]
	[[Category: Acetazolamide]]		[[Category: Acetazolamide]]
	[[Category: Carbon dioxide capture]]		[[Category: Carbon dioxide capture]]

OCA at 08:30, 20 October 2014

OCA — Mon, 20 Oct 2014 08:30:36 GMT

←Older revision		Revision as of 08:30, 20 October 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t 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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilic Thermovibrio ammonificans alpha-carbonic anhydrase (TaCA) has been expressed in Escherichia coli and structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of the E. coli host cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70 degrees C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized alpha-carbonic anhydrases, TaCA does not display esterase activity towards p-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.
		+
		+	The structure of a tetrameric alpha-carbonic anhydrase from Thermovibrio ammonificans reveals a core formed around intermolecular disulfides that contribute to its thermostability.,James P, Isupov MN, Sayer C, Saneei V, Berg S, Lioliou M, Kotlar HK, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2607-18. doi:, 10.1107/S1399004714016526. Epub 2014 Sep 27. PMID:25286845<ref>PMID:25286845</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:05, 10 September 2014

OCA — Wed, 10 Sep 2014 10:05:25 GMT

←Older revision		Revision as of 10:05, 10 September 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme==
-		+	<StructureSection load='4c3t' size='340' side='right' caption='[[4c3t]], [[Resolution\|resolution]] 1.69Å' scene=''>
-	~~The entry~~ 4c3t is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br>
-	~~Authors~~: ~~James~~, P.~~, Isupov, M~~., ~~Sayer~~, C., Berg, S.~~, Lioliou~~, M., Kotlar, H., Littlechild, J.	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
-		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></td></tr>
-	~~Description~~: ~~The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal~~ stability ~~of this enzyme~~	+	<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=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Carbonate dehydratase]]
		+	[[Category: Thermovibrio ammonificans]]
		+	[[Category: Berg, S.]]
		+	[[Category: Isupov, M.]]
		+	[[Category: James, P.]]
		+	[[Category: Kotlar, H.]]
		+	[[Category: Lioliou, M.]]
		+	[[Category: Littlechild, J.]]
		+	[[Category: Sayer, C.]]
		+	[[Category: Acetazolamide]]
		+	[[Category: Carbon dioxide capture]]
		+	[[Category: Lyase]]
		+	[[Category: Thermal stability]]
		+	[[Category: Thermophilic]]

OCA at 11:42, 12 March 2014

OCA — Wed, 12 Mar 2014 11:42:17 GMT

←Older revision		Revision as of 11:42, 12 March 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c3t is ON HOLD	+	The entry 4c3t is ON HOLD until Paper Publication

	Authors: James, P., Isupov, M., Sayer, C., Berg, S., Lioliou, M., Kotlar, H., Littlechild, J.		Authors: James, P., Isupov, M., Sayer, C., Berg, S., Lioliou, M., Kotlar, H., Littlechild, J.

	Description: The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme		Description: The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme

OCA at 06:31, 2 October 2013

OCA — Wed, 02 Oct 2013 06:31:50 GMT

←Older revision		Revision as of 06:31, 2 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c3t is ON HOLD ~~until Paper Publication~~	+	The entry 4c3t is ON HOLD

	Authors: James, P., Isupov, M., Sayer, C., Berg, S., Lioliou, M., Kotlar, H., Littlechild, J.		Authors: James, P., Isupov, M., Sayer, C., Berg, S., Lioliou, M., Kotlar, H., Littlechild, J.

	Description: The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme		Description: The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme

OCA: Protected "4c3t" [edit=sysop:move=sysop]

OCA — Wed, 04 Sep 2013 09:32:02 GMT

Protected "4c3t" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:32, 4 September 2013