1m7t - Revision history

OCA at 08:32, 10 April 2024

OCA — Wed, 10 Apr 2024 08:32:40 GMT

←Older revision		Revision as of 08:32, 10 April 2024
Line 1:		Line 1:

	==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==		==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==
-	<StructureSection load='1m7t' size='340' side='right'caption='[[1m7t~~]], [[NMR_Ensembles_of_Models \| 21 NMR models~~]]' scene=''>	+	<StructureSection load='1m7t' size='340' side='right'caption='[[1m7t]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
-	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [https://pdbe.org/1m7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [https://www.ebi.ac.uk/pdbsum/1m7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7t ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [https://pdbe.org/1m7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [https://www.ebi.ac.uk/pdbsum/1m7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>	+	[https://www.uniprot.org/uniprot/THIO_ECOLI THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== 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=1m7t 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=1m7t ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We have determined the high-resolution solution structure of the oxidized form of a chimeric human and Escherichia coli thioredoxin (TRX(HE)) by NMR. The overall structure is well-defined with a rms difference for the backbone atoms of 0.27 +/- 0.06 A. The topology of the protein is identical to those of the human and E. coli parent proteins, consisting of a central five-stranded beta-sheet surrounded by four alpha-helices. Analysis of the interfaces between the two domains derived from the human and E. coli sequences reveals that the general hydrophobic packing is unaltered and only subtle changes in the details of side chain interactions are observed. The packing of helix alpha(4) with helix alpha(2) across the hybrid interface is less optimal than in the parent molecules, and electrostatic interactions between polar side chains are missing. In particular, lysine-glutamate salt bridges between residues on helices alpha(2) and alpha(4), which were observed in both human and E. coli proteins, are not present in the chimeric protein. The origin of the known reduced thermodynamic stability of TRX(HE) was probed by mutagenesis on the basis of these structural findings. Two mutants of TRX(HE), S44D and S44E, were created, and their thermal and chemical stabilities were examined. Improved stability toward chaotropic agents was observed for both mutants, but no increase in the denaturation temperature was seen compared to that of TRX(HE). In addition to the structural analysis, the backbone dynamics of TRX(HE) were investigated by (15)N NMR relaxation measurements. Analysis using the model free approach reveals that the protein is fairly rigid with an average S(2) of 0.88. Increased mobility is primarily present in two external loop regions comprising residues 72-74 and 92-94 that contain glycine and proline residues.
-
-	Solution structure and dynamics of the human-Escherichia coli thioredoxin chimera: insights into thermodynamic stability.,Dangi B, Dobrodumov AV, Louis JM, Gronenborn AM Biochemistry. 2002 Jul 30;41(30):9376-88. PMID:12135359<ref>PMID:12135359</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1m7t" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Escherichia coli]]
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dangi, B]]	+	[[Category: Dangi B]]
-	[[Category: Dobrodumov~~, A V~~]]	+	[[Category: Dobrodumov AV]]
-	[[Category: Gronenborn~~, A M~~]]	+	[[Category: Gronenborn AM]]
-	[[Category: Louis~~, J M]]~~	+	[[Category: Louis JM]]
-	~~[[Category: Chimera]]~~	+
-	~~[[Category: Dynamic]]~~	+
-	~~[[Category: E. coli]]~~	+
-	~~[[Category: Electron transport]]~~	+
-	~~[[Category: Stability~~]]	+

OCA at 06:53, 18 August 2021

OCA — Wed, 18 Aug 2021 06:53:49 GMT

←Older revision		Revision as of 06:53, 18 August 2021
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	<StructureSection load='1m7t' size='340' side='right'caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>		<StructureSection load='1m7t' size='340' side='right'caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1M7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
-	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [~~http~~://pdbe.org/1m7t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1m7t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7t ProSAT]</span></td></tr>	+	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [https://pdbe.org/1m7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [https://www.ebi.ac.uk/pdbsum/1m7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>	+	[[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 29:		Line 29:

	==See Also==		==See Also==
-	*[[Thioredoxin\|Thioredoxin]]	+	*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:18, 13 November 2019

OCA — Wed, 13 Nov 2019 12:18:16 GMT

←Older revision		Revision as of 12:18, 13 November 2019
Line 1:		Line 1:

	==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==		==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==
-	<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>	+	<StructureSection load='1m7t' size='340' side='right'caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
Line 27:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1m7t" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1m7t" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Dangi, B]]		[[Category: Dangi, B]]
	[[Category: Dobrodumov, A V]]		[[Category: Dobrodumov, A V]]

OCA at 07:54, 31 January 2018

OCA — Wed, 31 Jan 2018 07:54:13 GMT

←Older revision		Revision as of 07:54, 31 January 2018
Line 1:		Line 1:
		+
	==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==		==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==
	<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>		<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
-	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://pdbe.org/1m7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum]</span></td></tr>	+	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://pdbe.org/1m7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 11:		Line 12:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/1m7t_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/1m7t_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>
Line 26:		Line 27:
	</div>		</div>
	<div class="pdbe-citations 1m7t" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1m7t" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:11, 9 February 2016

OCA — Tue, 09 Feb 2016 22:11:08 GMT

←Older revision		Revision as of 22:11, 9 February 2016
Line 15:		Line 15:
	<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=1m7t ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:31, 11 September 2015

OCA — Fri, 11 Sep 2015 02:31:24 GMT

←Older revision		Revision as of 02:31, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>		<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia coli~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
-	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum]</span></td></tr>	+	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://pdbe.org/1m7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 25:		Line 25:
	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 1m7t" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia coli~~]]	+	[[Category: Human]]
	[[Category: Dangi, B]]		[[Category: Dangi, B]]
	[[Category: Dobrodumov, A V]]		[[Category: Dobrodumov, A V]]
Line 41:		Line 42:
	[[Category: E. coli]]		[[Category: E. coli]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
-	[[Category: Human]]
	[[Category: Stability]]		[[Category: Stability]]

OCA at 09:52, 25 December 2014

OCA — Thu, 25 Dec 2014 09:52:34 GMT

←Older revision		Revision as of 09:52, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
-	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum]</span></td></tr>	+	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
-	[[Category: Dangi, B.]]	+	[[Category: Dangi, B]]
-	[[Category: Dobrodumov, A V.]]	+	[[Category: Dobrodumov, A V]]
-	[[Category: Gronenborn, A M.]]	+	[[Category: Gronenborn, A M]]
-	[[Category: Louis, J M.]]	+	[[Category: Louis, J M]]
	[[Category: Chimera]]		[[Category: Chimera]]
	[[Category: Dynamic]]		[[Category: Dynamic]]

OCA at 16:02, 28 September 2014

OCA — Sun, 28 Sep 2014 16:02:56 GMT

←Older revision		Revision as of 16:02, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1m7t.~~png\|left~~\|200px]]	+	==Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability==
		+	<StructureSection load='1m7t' size='340' side='right' caption='[[1m7t]], [[NMR_Ensembles_of_Models \| 21 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M7T FirstGlance]. <br>
		+	</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=1m7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m7t RCSB], [http://www.ebi.ac.uk/pdbsum/1m7t 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/m7/1m7t_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 ==
		+	We have determined the high-resolution solution structure of the oxidized form of a chimeric human and Escherichia coli thioredoxin (TRX(HE)) by NMR. The overall structure is well-defined with a rms difference for the backbone atoms of 0.27 +/- 0.06 A. The topology of the protein is identical to those of the human and E. coli parent proteins, consisting of a central five-stranded beta-sheet surrounded by four alpha-helices. Analysis of the interfaces between the two domains derived from the human and E. coli sequences reveals that the general hydrophobic packing is unaltered and only subtle changes in the details of side chain interactions are observed. The packing of helix alpha(4) with helix alpha(2) across the hybrid interface is less optimal than in the parent molecules, and electrostatic interactions between polar side chains are missing. In particular, lysine-glutamate salt bridges between residues on helices alpha(2) and alpha(4), which were observed in both human and E. coli proteins, are not present in the chimeric protein. The origin of the known reduced thermodynamic stability of TRX(HE) was probed by mutagenesis on the basis of these structural findings. Two mutants of TRX(HE), S44D and S44E, were created, and their thermal and chemical stabilities were examined. Improved stability toward chaotropic agents was observed for both mutants, but no increase in the denaturation temperature was seen compared to that of TRX(HE). In addition to the structural analysis, the backbone dynamics of TRX(HE) were investigated by (15)N NMR relaxation measurements. Analysis using the model free approach reveals that the protein is fairly rigid with an average S(2) of 0.88. Increased mobility is primarily present in two external loop regions comprising residues 72-74 and 92-94 that contain glycine and proline residues.

-	~~{{STRUCTURE_1m7t\| PDB=1m7t \| SCENE= }}~~	+	Solution structure and dynamics of the human-Escherichia coli thioredoxin chimera: insights into thermodynamic stability.,Dangi B, Dobrodumov AV, Louis JM, Gronenborn AM Biochemistry. 2002 Jul 30;41(30):9376-88. PMID:12135359<ref>PMID:12135359</ref>

-	~~===Solution Structure and Dynamics~~ of the ~~Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12135359}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1m7t]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA].~~	+

	==See Also==		==See Also==
	*[[Thioredoxin\|Thioredoxin]]		*[[Thioredoxin\|Thioredoxin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012135359<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Dangi, B.]]		[[Category: Dangi, B.]]

OCA at 15:18, 20 October 2012

OCA — Sat, 20 Oct 2012 15:18:59 GMT

←Older revision		Revision as of 15:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1m7t]] is a 1 chain structure ~~of [[Thioredoxin]]~~ with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens,_escherichia_coli Homo sapiens, escherichia~~ coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA].	+	[[1m7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA].

	==See Also==		==See Also==
Line 15:		Line 15:
	==Reference==		==Reference==
	<ref group="xtra">PMID:012135359</ref><references group="xtra"/>		<ref group="xtra">PMID:012135359</ref><references group="xtra"/>
-	[[Category: ~~Homo sapiens, escherichia~~ coli]]	+	[[Category: Escherichia coli]]
	[[Category: Dangi, B.]]		[[Category: Dangi, B.]]
	[[Category: Dobrodumov, A V.]]		[[Category: Dobrodumov, A V.]]

OCA at 17:59, 26 July 2012

OCA — Thu, 26 Jul 2012 17:59:55 GMT

←Older revision		Revision as of 17:59, 26 July 2012
Line 1:		Line 1:
	[[Image:1m7t.png\|left\|200px]]		[[Image:1m7t.png\|left\|200px]]

-	<!--
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-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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	{{STRUCTURE_1m7t\| PDB=1m7t \| SCENE= }}		{{STRUCTURE_1m7t\| PDB=1m7t \| SCENE= }}

	===Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability===		===Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12135359}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12135359 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_12135359}}		{{ABSTRACT_PUBMED_12135359}}

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	==See Also==		==See Also==
-	*[[Thioredoxin]]	+	*[[Thioredoxin\|Thioredoxin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12135359~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012135359</ref><references group="xtra"/>
	[[Category: Homo sapiens, escherichia coli]]		[[Category: Homo sapiens, escherichia coli]]
	[[Category: Dangi, B.]]		[[Category: Dangi, B.]]