1gl8 - Revision history

OCA at 11:22, 27 March 2024

2024-03-27T11:22:21Z

←Older revision		Revision as of 11:22, 27 March 2024
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	==Solution structure of thioredoxin m from spinach, oxidized form==		==Solution structure of thioredoxin m from spinach, oxidized form==
-	<StructureSection load='1gl8' size='340' side='right'caption='[[1gl8~~]], [[NMR_Ensembles_of_Models \| 25 NMR models~~]]' scene=''>	+	<StructureSection load='1gl8' size='340' side='right'caption='[[1gl8]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Spiol Spiol~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1fb0\|1fb0]], [[1fb6\|1fb6]]</div~~></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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [https://pdbe.org/1gl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl8 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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [https://pdbe.org/1gl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.	+	[https://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
	== 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=1gl8 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=1gl8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Proton NMR spectral resonances of thioredoxin m from spinach have been assigned, and its solution structure has been determined on the basis of 1156 nuclear Overhauser effect- (NOE-) derived distance constraints by using restrained molecular dynamics calculations. The average pairwise root-mean-square deviation (RMSD) for the 25 best NMR structures for the backbone was 1.0 +/- 0.1, when the structurally well-defined residues were considered. The N- and C-terminal segments (1-13 and 118-119) and residues 41-49, comprising the active site, are highly disordered. At the time of concluding this work, a crystal structure of this protein was reported, in which thioredoxin m was found to crystallize as noncovalent dimers. Although the solution and crystal structures are very similar, no evidence was found about the existence of dimers in solution, thus confirming that dimerization is not needed for the regulatory activity of thioredoxin m. The spinach thioredoxin m does not unfold by heat in the range 25-85 degrees C, as revealed by thermal circular dichroic (CD) measurements. However, its unfolding free energy (9.1 +/- 0.8 kcal mol(-1), at pH 5.3 and 25 degrees C) could be determined by extrapolating the free energy values obtained at different concentrations of guanidinium chloride (GdmCl). The folding-unfolding process is two-state as indicated by the coincidence of the CD denaturation curves obtained at far and near UV. The H/D exchange behavior of backbone amide protons was analyzed. The slowest-exchanging protons, requiring a global-unfolding mechanism in order to exchange, are those from beta2, beta3, and beta4, the central strands of the beta-sheet, which constitute the main element of the core of the protein. The free energies obtained from exchange measurements of protons belonging to the alpha-helices are lower than those derived from GdmCl denaturation studies, indicating that those protons exchange by local-unfolding mechanisms.
-
-	Three-dimensional solution structure and stability of thioredoxin m from spinach.,Neira JL, Gonzalez C, Toiron C, de Prat-Gay G, Rico M Biochemistry. 2001 Dec 18;40(50):15246-56. PMID:11735407<ref>PMID:11735407</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1gl8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]		*[[Thioredoxin 3D structures\|Thioredoxin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Spiol~~]]	+	[[Category: Spinacia oleracea]]
-	[[Category: De-Prat-gay, G]]	+	[[Category: De-Prat-gay G]]
-	[[Category: Gonzalez, C]]	+	[[Category: Gonzalez C]]
-	[[Category: Neira~~, J L~~]]	+	[[Category: Neira JL]]
-	[[Category: Rico, M]]	+	[[Category: Rico M]]
-	[[Category: Toiron, C]]	+	[[Category: Toiron C]]
-	~~[[Category: Electron transport]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Redox-active center~~]]	+

OCA at 11:25, 28 July 2021

2021-07-28T11:25:19Z

←Older revision		Revision as of 11:25, 28 July 2021
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	<StructureSection load='1gl8' size='340' side='right'caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1gl8' size='340' side='right'caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fb0\|1fb0]], [[1fb6\|1fb6]]</div></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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [~~http~~://pdbe.org/1gl8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1gl8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl8 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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [https://pdbe.org/1gl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.	+	[[https://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:

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

OCA at 08:39, 23 October 2019

2019-10-23T08:39:31Z

←Older revision		Revision as of 08:39, 23 October 2019
Line 1:		Line 1:

	==Solution structure of thioredoxin m from spinach, oxidized form==		==Solution structure of thioredoxin m from spinach, oxidized form==
-	<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>	+	<StructureSection load='1gl8' size='340' side='right'caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
Line 28:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1gl8" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1gl8" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Spiol]]		[[Category: Spiol]]
	[[Category: De-Prat-gay, G]]		[[Category: De-Prat-gay, G]]

OCA at 06:24, 3 January 2018

2018-01-03T06:24:47Z

←Older revision		Revision as of 06:24, 3 January 2018
Line 1:		Line 1:
-	==~~SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH~~, ~~OXIDIZED FORM~~==	+
		+	==Solution structure of thioredoxin m from spinach, oxidized form==
	<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://pdbe.org/1gl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://pdbe.org/1gl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gl8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1gl8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1gl8_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 27:		Line 28:
	</div>		</div>
	<div class="pdbe-citations 1gl8" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1gl8" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thioredoxin\|Thioredoxin]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Spiol]]		[[Category: Spiol]]
-	[[Category: De-Prat-~~Gay~~, G]]	+	[[Category: De-Prat-gay, G]]
	[[Category: Gonzalez, C]]		[[Category: Gonzalez, C]]
	[[Category: Neira, J L]]		[[Category: Neira, J L]]

OCA at 20:15, 9 February 2016

2016-02-09T20:15:34Z

←Older revision		Revision as of 20:15, 9 February 2016
Line 16:		Line 16:
	<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=1gl8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 01:40, 11 September 2015

2015-09-11T01:40:10Z

←Older revision		Revision as of 01:40, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>		<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Spinacia_oleracea Spinacia oleracea~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spiol Spiol]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://pdbe.org/1gl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRXM_SPIOL TRXM_SPIOL]] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	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 1gl8" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 31:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Spinacia oleracea~~]]	+	[[Category: Spiol]]
	[[Category: De-Prat-Gay, G]]		[[Category: De-Prat-Gay, G]]
	[[Category: Gonzalez, C]]		[[Category: Gonzalez, C]]

OCA at 21:55, 22 December 2014

2014-12-22T21:55:58Z

←Older revision		Revision as of 21:55, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 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 32:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Spinacia oleracea]]		[[Category: Spinacia oleracea]]
-	[[Category: De-Prat-Gay, G.]]	+	[[Category: De-Prat-Gay, G]]
-	[[Category: Gonzalez, C.]]	+	[[Category: Gonzalez, C]]
-	[[Category: Neira, J L.]]	+	[[Category: Neira, J L]]
-	[[Category: Rico, M.]]	+	[[Category: Rico, M]]
-	[[Category: Toiron, C.]]	+	[[Category: Toiron, C]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Redox-active center]]		[[Category: Redox-active center]]

OCA at 11:48, 28 September 2014

2014-09-28T11:48:38Z

←Older revision		Revision as of 11:48, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1gl8.~~png~~\|~~left~~\|200px]]	+	==SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM==
		+	<StructureSection load='1gl8' size='340' side='right' caption='[[1gl8]], [[NMR_Ensembles_of_Models \| 25 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GL8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fb0\|1fb0]], [[1fb6\|1fb6]]</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=1gl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gl8 RCSB], [http://www.ebi.ac.uk/pdbsum/1gl8 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/gl/1gl8_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 ==
		+	Proton NMR spectral resonances of thioredoxin m from spinach have been assigned, and its solution structure has been determined on the basis of 1156 nuclear Overhauser effect- (NOE-) derived distance constraints by using restrained molecular dynamics calculations. The average pairwise root-mean-square deviation (RMSD) for the 25 best NMR structures for the backbone was 1.0 +/- 0.1, when the structurally well-defined residues were considered. The N- and C-terminal segments (1-13 and 118-119) and residues 41-49, comprising the active site, are highly disordered. At the time of concluding this work, a crystal structure of this protein was reported, in which thioredoxin m was found to crystallize as noncovalent dimers. Although the solution and crystal structures are very similar, no evidence was found about the existence of dimers in solution, thus confirming that dimerization is not needed for the regulatory activity of thioredoxin m. The spinach thioredoxin m does not unfold by heat in the range 25-85 degrees C, as revealed by thermal circular dichroic (CD) measurements. However, its unfolding free energy (9.1 +/- 0.8 kcal mol(-1), at pH 5.3 and 25 degrees C) could be determined by extrapolating the free energy values obtained at different concentrations of guanidinium chloride (GdmCl). The folding-unfolding process is two-state as indicated by the coincidence of the CD denaturation curves obtained at far and near UV. The H/D exchange behavior of backbone amide protons was analyzed. The slowest-exchanging protons, requiring a global-unfolding mechanism in order to exchange, are those from beta2, beta3, and beta4, the central strands of the beta-sheet, which constitute the main element of the core of the protein. The free energies obtained from exchange measurements of protons belonging to the alpha-helices are lower than those derived from GdmCl denaturation studies, indicating that those protons exchange by local-unfolding mechanisms.

-	~~{{STRUCTURE_1gl8\| PDB=1gl8 \| SCENE= }}~~	+	Three-dimensional solution structure and stability of thioredoxin m from spinach.,Neira JL, Gonzalez C, Toiron C, de Prat-Gay G, Rico M Biochemistry. 2001 Dec 18;40(50):15246-56. PMID:11735407<ref>PMID:11735407</ref>

-	~~===SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH~~, ~~OXIDIZED FORM===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11735407}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1gl8]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Spinacia_oleracea Spinacia oleracea]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA].~~	+

	==See Also==		==See Also==
	*[[Thioredoxin\|Thioredoxin]]		*[[Thioredoxin\|Thioredoxin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:011735407<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Spinacia oleracea]]		[[Category: Spinacia oleracea]]
	[[Category: De-Prat-Gay, G.]]		[[Category: De-Prat-Gay, G.]]

OCA at 15:00, 20 October 2012

2012-10-20T15:00:31Z

←Older revision		Revision as of 15:00, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1gl8]] is a 1 chain structure ~~of [[Thioredoxin]]~~ with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA].	+	[[1gl8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA].

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

OCA at 16:59, 26 July 2012

2012-07-26T16:59:02Z

←Older revision		Revision as of 16:59, 26 July 2012
Line 1:		Line 1:
	[[Image:1gl8.png\|left\|200px]]		[[Image:1gl8.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1gl8", 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.
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	{{STRUCTURE_1gl8\| PDB=1gl8 \| SCENE= }}		{{STRUCTURE_1gl8\| PDB=1gl8 \| SCENE= }}

	===SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM===		===SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11735407}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11735407 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_11735407}}		{{ABSTRACT_PUBMED_11735407}}

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11735407~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011735407</ref><references group="xtra"/>
	[[Category: Spinacia oleracea]]		[[Category: Spinacia oleracea]]
	[[Category: De-Prat-Gay, G.]]		[[Category: De-Prat-Gay, G.]]