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3tz1

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==Crystal structure of the Ca2+-saturated C-terminal domain of Akazara scallop troponin C in complex with a troponin I fragment==
==Crystal structure of the Ca2+-saturated C-terminal domain of Akazara scallop troponin C in complex with a troponin I fragment==
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<StructureSection load='3tz1' size='340' side='right' caption='[[3tz1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3tz1' size='340' side='right'caption='[[3tz1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tz1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamys_nipponensis_akazara Chlamys nipponensis akazara]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TZ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamys_nipponensis_akazara Chlamys nipponensis akazara]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TZ1 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Troponin C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6571 Chlamys nipponensis akazara])</td></tr>
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<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>
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<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=3tz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tz1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tz1 RCSB], [http://www.ebi.ac.uk/pdbsum/3tz1 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tz1 OCA], [https://pdbe.org/3tz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tz1 RCSB], [https://www.ebi.ac.uk/pdbsum/3tz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tz1 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q27428_CHLNI Q27428_CHLNI]
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Abstract Troponin C (TnC) is the Ca2+-sensing subunit of troponin that triggers the contraction of striated muscles. In scallops, the striated muscles consume little ATP energy in sustaining strong contractile forces. The N-terminal domain of TnC works as the Ca2+ sensor in vertebrates, whereas scallop TnC uses the C-terminal domain as the Ca2+ sensor, suggesting that there are differences in the mechanism of the Ca2+-dependent regulation of muscles between invertebrates and vertebrates. Here, we report the crystal structure of the Akazara scallop adductor muscle TnC C-terminal domain (asTnCC) complexed with a short troponin I fragment (asTnIS) and Ca2+. The electron density of a Ca2+ ion is observed in only one of the two EF-hands. The EF-hands of asTnCC can only be in the fully open conformation with the assistance of asTnIS. The number of hydrogen bonds between asTnCC and asTnIS is markedly lower than the number in the vertebrate counterparts. The Ca2+ modulation on the binding between asTnCC and asTnIS is weaker, but structural change of the complex depending on Ca2+ concentration was observed. Together, these findings provide a detailed description of the distinct molecular mechanism of contractile regulation in the scallop adductor muscle from that of vertebrates.
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Structure of the Ca2+-saturated C-terminal domain of scallop troponin C in complex with a troponin I fragment.,Kato YS, Yumoto F, Tanaka H, Miyakawa T, Miyauchi Y, Takeshita D, Sawano Y, Ojima T, Ohtsuki I, Tanokura M Biol Chem. 2012 Aug 4. pii:, /j/bchm.just-accepted/hsz-2012-0152/hsz-2012-0152.xml. doi:, 10.1515/hsz-2012-0152. PMID:23096565<ref>PMID:23096565</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Troponin|Troponin]]
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*[[Troponin 3D structures|Troponin 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chlamys nipponensis akazara]]
[[Category: Chlamys nipponensis akazara]]
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[[Category: Kato, Y S]]
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[[Category: Large Structures]]
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[[Category: Ohtsuki, I]]
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[[Category: Kato YS]]
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[[Category: Tanokura, M]]
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[[Category: Ohtsuki I]]
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[[Category: Yumoto, F]]
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[[Category: Tanokura M]]
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[[Category: Ca2+-sensor]]
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[[Category: Yumoto F]]
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[[Category: Contractile protein]]
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[[Category: Ef hand]]
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[[Category: Protein-peptide complex]]
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Current revision

Crystal structure of the Ca2+-saturated C-terminal domain of Akazara scallop troponin C in complex with a troponin I fragment

PDB ID 3tz1

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