5tnc - Revision history

OCA at 14:22, 6 March 2024

2024-03-06T14:22:31Z

←Older revision		Revision as of 14:22, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='5tnc' size='340' side='right'caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5tnc' size='340' side='right'caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Melga Melga~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5TNC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TNC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [~~http~~://pdbe.org/5tnc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tnc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnc ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [https://pdbe.org/5tnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [https://www.ebi.ac.uk/pdbsum/5tnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TNNC2_MELGA TNNC2_MELGA]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.	+	[https://www.uniprot.org/uniprot/TNNC2_MELGA TNNC2_MELGA] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 20:
	</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=5tnc 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=5tnc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The crystal structure of troponin C from turkey skeletal muscle has been refined at 2.0 A resolution (1 A = 0.1 nm). The resulting crystallographic R factor (R = sigma[[Fo[-[Fc[[/sigma[Fo[, where [Fo[ and [Fc[ are the observed and calculated structure factor amplitudes) is 0.155 for the 8054 reflections with intensities I greater than or equal to 2 sigma(I) within the 10 A to 2.0 A resolution range. With 66% of the residues in helical conformation, troponin C provides a good sample for helix analysis. The mean alpha-helix dihedral angles (phi, psi = -62 degrees, -42 degrees) agree with values observed for helical regions in other proteins. The helices are all curved and/or kinked. In particular, the 31 amino acid long inter-domain helix is smoothly curved, with a rather large radius of curvature of 137 A. Helix packing is different in the Ca2+-free domain (N-terminal) and the Ca2+-bound domain (C-terminal). The inter-helix angles for the two helix-loop-helix motifs in the regulatory domain are 133 degrees and 151 degrees, whereas the value for the two motifs in the C-terminal domain is 110 degrees, as observed in the EF-hands of parvalbumin. These differences affect the packing of the respective hydrophobic cores of each domain, in particular the disposition of aromatic rings. Pairwise arrangement of Ca2+-binding loops is common to both states, but the conformation is markedly different. Conversion of one to the other can be achieved by small cumulative changes of main-chain dihedral angles. The integrity of loop structure is maintained by numerous electrostatic interactions. Both salt bridges and carboxyl-carboxylate interactions are observed in TnC. There are more intramolecular (9) than intermolecular (1) salt bridges. Carboxyl-carboxylate interactions occur because the pH of the crystals is 5.0 and there is a multitude of aspartate and glutamate residues. One is intramolecular and four are intermolecular. Polar side-chain interactions occur more commonly with main-chain carbonyls and amides than with other polar side-chains. These interactions are mostly short range, and are similar to those observed in other proteins with one exception: negatively charged side-chains interact more frequently with main-chain carbonyl oxygen atoms. However, out of 19 such interactions, 10 involve oxygen atoms of the Ca2+ ligands. These unfavorable interactions are compensated by the favorable interactions with the Ca2+ ions and with main-chain amides. They are a trivial consequence of the tight fold of the Ca2+-binding loops.
-
-	Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resolution.,Herzberg O, James MN J Mol Biol. 1988 Oct 5;203(3):761-79. PMID:3210231<ref>PMID:3210231</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5tnc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Troponin\|Troponin]]	+	*[[Troponin 3D structures\|Troponin 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Melga~~]]	+	[[Category: Meleagris gallopavo]]
-	[[Category: Herzberg, O]]	+	[[Category: Herzberg O]]
-	[[Category: James~~, M N.G]]~~	+	[[Category: James MNG]]
-	~~[[Category: Contractile system protein~~]]	+

OCA at 12:14, 23 September 2020

2020-09-23T12:14:19Z

←Older revision		Revision as of 12:14, 23 September 2020
Line 1:		Line 1:

	==REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION==		==REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION==
-	<StructureSection load='5tnc' size='340' side='right' caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='5tnc' size='340' side='right'caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Common_turkey Common turkey~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TNC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Melga Melga]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TNC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://pdbe.org/5tnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnc ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://pdbe.org/5tnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tn/5tnc_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tn/5tnc_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 35:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Common turkey~~]]	+	[[Category: Large Structures]]
		+	[[Category: Melga]]
	[[Category: Herzberg, O]]		[[Category: Herzberg, O]]
	[[Category: James, M N.G]]		[[Category: James, M N.G]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]

OCA at 08:19, 5 August 2016

2016-08-05T08:19:21Z

←Older revision		Revision as of 08:19, 5 August 2016
Line 1:		Line 1:
		+
	==REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION==		==REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION==
	<StructureSection load='5tnc' size='340' side='right' caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='5tnc' size='340' side='right' caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Meleagris_gallopavo Meleagris gallopavo~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_turkey Common turkey]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc 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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://pdbe.org/5tnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tnc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	<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=5tnc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 26:		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 5tnc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Meleagris gallopavo~~]]	+	[[Category: Common turkey]]
	[[Category: Herzberg, O]]		[[Category: Herzberg, O]]
	[[Category: James, M N.G]]		[[Category: James, M N.G]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]

OCA at 17:12, 25 December 2014

2014-12-25T17:12:48Z

←Older revision		Revision as of 17:12, 25 December 2014
Line 6:		Line 6:
	<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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc 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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TNNC2_MELGA TNNC2_MELGA]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:58, 10 December 2014

2014-12-10T16:58:33Z

←Older revision		Revision as of 16:58, 10 December 2014
Line 1:		Line 1:
-	[[~~Image~~:5tnc.~~png\|left~~\|200px]]	+	==REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION==
		+	<StructureSection load='5tnc' size='340' side='right' caption='[[5tnc]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TNC FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5tnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5tnc RCSB], [http://www.ebi.ac.uk/pdbsum/5tnc 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/tn/5tnc_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 ==
		+	The crystal structure of troponin C from turkey skeletal muscle has been refined at 2.0 A resolution (1 A = 0.1 nm). The resulting crystallographic R factor (R = sigma[[Fo[-[Fc[[/sigma[Fo[, where [Fo[ and [Fc[ are the observed and calculated structure factor amplitudes) is 0.155 for the 8054 reflections with intensities I greater than or equal to 2 sigma(I) within the 10 A to 2.0 A resolution range. With 66% of the residues in helical conformation, troponin C provides a good sample for helix analysis. The mean alpha-helix dihedral angles (phi, psi = -62 degrees, -42 degrees) agree with values observed for helical regions in other proteins. The helices are all curved and/or kinked. In particular, the 31 amino acid long inter-domain helix is smoothly curved, with a rather large radius of curvature of 137 A. Helix packing is different in the Ca2+-free domain (N-terminal) and the Ca2+-bound domain (C-terminal). The inter-helix angles for the two helix-loop-helix motifs in the regulatory domain are 133 degrees and 151 degrees, whereas the value for the two motifs in the C-terminal domain is 110 degrees, as observed in the EF-hands of parvalbumin. These differences affect the packing of the respective hydrophobic cores of each domain, in particular the disposition of aromatic rings. Pairwise arrangement of Ca2+-binding loops is common to both states, but the conformation is markedly different. Conversion of one to the other can be achieved by small cumulative changes of main-chain dihedral angles. The integrity of loop structure is maintained by numerous electrostatic interactions. Both salt bridges and carboxyl-carboxylate interactions are observed in TnC. There are more intramolecular (9) than intermolecular (1) salt bridges. Carboxyl-carboxylate interactions occur because the pH of the crystals is 5.0 and there is a multitude of aspartate and glutamate residues. One is intramolecular and four are intermolecular. Polar side-chain interactions occur more commonly with main-chain carbonyls and amides than with other polar side-chains. These interactions are mostly short range, and are similar to those observed in other proteins with one exception: negatively charged side-chains interact more frequently with main-chain carbonyl oxygen atoms. However, out of 19 such interactions, 10 involve oxygen atoms of the Ca2+ ligands. These unfavorable interactions are compensated by the favorable interactions with the Ca2+ ions and with main-chain amides. They are a trivial consequence of the tight fold of the Ca2+-binding loops.

-	~~{{STRUCTURE_5tnc\| PDB=5tnc \| SCENE= }}~~	+	Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 A resolution.,Herzberg O, James MN J Mol Biol. 1988 Oct 5;203(3):761-79. PMID:3210231<ref>PMID:3210231</ref>

-	~~===REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_3210231}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[5tnc]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes~~ the ~~now removed PDB entry [http://oca~~.~~weizmann~~.ac.il/~~oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA].~~	+

	==See Also==		==See Also==
	*[[Troponin\|Troponin]]		*[[Troponin\|Troponin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:003210231<~~/~~ref~~><~~ref group="xtra">PMID:015215457</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Meleagris gallopavo]]		[[Category: Meleagris gallopavo]]
-	[[Category: Herzberg, O.]]	+	[[Category: Herzberg, O]]
-	[[Category: James, M N.G.]]	+	[[Category: James, M N.G]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]

OCA at 19:19, 20 October 2012

2012-10-20T19:19:16Z

←Older revision		Revision as of 19:19, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[5tnc]] is a 1 chain structure ~~of [[Troponin]]~~ with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA].	+	[[5tnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA].

	==See Also==		==See Also==
Line 14:		Line 14:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:003210231~~</ref><ref group="xtra">PMID:010933496~~</ref><ref group="xtra">PMID:015215457</ref><references group="xtra"/>	+	<ref group="xtra">PMID:003210231</ref><ref group="xtra">PMID:015215457</ref><references group="xtra"/>
	[[Category: Meleagris gallopavo]]		[[Category: Meleagris gallopavo]]
	[[Category: Herzberg, O.]]		[[Category: Herzberg, O.]]
	[[Category: James, M N.G.]]		[[Category: James, M N.G.]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]

OCA at 06:58, 27 July 2012

2012-07-27T06:58:02Z

←Older revision		Revision as of 06:58, 27 July 2012
Line 1:		Line 1:
	[[Image:5tnc.png\|left\|200px]]		[[Image:5tnc.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_5tnc", 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_5tnc\| PDB=5tnc \| SCENE= }}		{{STRUCTURE_5tnc\| PDB=5tnc \| SCENE= }}

	===REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION===		===REFINED CRYSTAL STRUCTURE OF TROPONIN C FROM TURKEY SKELETAL MUSCLE AT 2.0 ANGSTROMS RESOLUTION===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_3210231}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 3210231 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_3210231}}		{{ABSTRACT_PUBMED_3210231}}

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~3210231~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:003210231</ref><ref group="xtra">PMID:010933496</ref><ref group="xtra">PMID:015215457</ref><references group="xtra"/>
	[[Category: Meleagris gallopavo]]		[[Category: Meleagris gallopavo]]
	[[Category: Herzberg, O.]]		[[Category: Herzberg, O.]]
	[[Category: James, M N.G.]]		[[Category: James, M N.G.]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]

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

2010-12-26T23:55:59Z

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

←Older revision

Revision as of 23:55, 26 December 2010

OCA at 23:55, 26 December 2010

2010-12-26T23:55:57Z

←Older revision		Revision as of 23:55, 26 December 2010
Line 1:		Line 1:
-	{{Seed}}
	[[Image:5tnc.png\|left\|200px]]		[[Image:5tnc.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~5TNC~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA].	+	[[5tnc]] is a 1 chain structure of [[Troponin]] with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tnc 2tnc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TNC OCA].
		+
		+	==See Also==
		+	*[[Troponin]]

	==Reference==		==Reference==
Line 28:		Line 30:
	[[Category: James, M N.G.]]		[[Category: James, M N.G.]]
	[[Category: Contractile system protein]]		[[Category: Contractile system protein]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jan 18 08:38:55 2010''

OCA: New page: {{Seed}} 200px