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==CALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR, 40 STRUCTURES== | |||
<StructureSection load='1smg' size='340' side='right'caption='[[1smg]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1smg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SMG FirstGlance]. <br> | |||
</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='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=1smg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smg OCA], [https://pdbe.org/1smg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1smg RCSB], [https://www.ebi.ac.uk/pdbsum/1smg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1smg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TNNC2_CHICK TNNC2_CHICK] 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 == | |||
[[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/sm/1smg_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/main_output.php?pdb_ID=1smg ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structural transition in troponin C induced by the binding of two calcium ions involves an "opening" of the structure, an event that triggers skeletal muscle contraction. We have solved the solution structure of a mutant (E41A) of the regulatory domain of skeletal troponin C wherein one bidentate ligand to the calcium in site I is missing. This structure remains "closed" upon calcium binding, indicating that the linkage between calcium binding and the induced conformational change has been broken. This provides a snapshot of skeletal troponin C between the off and on state and thereby valuable insight into the mechanism of regulation within skeletal TnC. Although several factors contribute to the triggering mechanism, the opening of the troponin C structure is ultimately dependent on one amino acid, Glu41. Insights into the structure of cardiac troponin C can also be derived from this skeletal mutant. | |||
Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins.,Gagne SM, Li MX, Sykes BD Biochemistry. 1997 Apr 15;36(15):4386-92. PMID:9109645<ref>PMID:9109645</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1smg" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Troponin|Troponin]] | *[[Troponin 3D structures|Troponin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Gagne SM]] | ||
[[Category: | [[Category: Li MX]] | ||
[[Category: | [[Category: Sykes BD]] | ||
Latest revision as of 12:09, 22 May 2024
CALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR, 40 STRUCTURESCALCIUM-BOUND E41A MUTANT OF THE N-DOMAIN OF CHICKEN TROPONIN C, NMR, 40 STRUCTURES
Structural highlights
FunctionTNNC2_CHICK 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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structural transition in troponin C induced by the binding of two calcium ions involves an "opening" of the structure, an event that triggers skeletal muscle contraction. We have solved the solution structure of a mutant (E41A) of the regulatory domain of skeletal troponin C wherein one bidentate ligand to the calcium in site I is missing. This structure remains "closed" upon calcium binding, indicating that the linkage between calcium binding and the induced conformational change has been broken. This provides a snapshot of skeletal troponin C between the off and on state and thereby valuable insight into the mechanism of regulation within skeletal TnC. Although several factors contribute to the triggering mechanism, the opening of the troponin C structure is ultimately dependent on one amino acid, Glu41. Insights into the structure of cardiac troponin C can also be derived from this skeletal mutant. Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins.,Gagne SM, Li MX, Sykes BD Biochemistry. 1997 Apr 15;36(15):4386-92. PMID:9109645[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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