9c1u
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM Structure of a Tm1C Fibril== | |
| + | <StructureSection load='9c1u' size='340' side='right'caption='[[9c1u]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9c1u]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9C1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C1U FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.31Å</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=9c1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c1u OCA], [https://pdbe.org/9c1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c1u RCSB], [https://www.ebi.ac.uk/pdbsum/9c1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c1u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q95TA3_DROME Q95TA3_DROME] Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.[ARBA:ARBA00002987] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The tropomyosin 1 isoform I/C C-terminal domain (Tm1-LC) fibril structure is studied jointly with cryogenic electron microscopy (cryo-EM) and solid state nuclear magnetic resonance (NMR). This study demonstrates the complementary nature of these two structural biology techniques. Chemical shift assignments from solid state NMR are used to determine the secondary structure at the level of individual amino acids, which is faithfully seen in cryo-EM reconstructions. Additionally, solid state NMR demonstrates that the region not observed in the reconstructed cryo-EM density is primarily in a highly mobile random coil conformation rather than adopting multiple rigid conformations. Overall, this study illustrates the benefit of investigations combining cryo-EM and solid state NMR to investigate protein fibril structure. | ||
| - | + | Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils.,Fonda BD, Kato M, Li Y, Murray DT Protein Sci. 2024 Oct;33(10):e5168. doi: 10.1002/pro.5168. PMID:39276003<ref>PMID:39276003</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9c1u" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fonda BD]] | ||
| + | [[Category: Kato M]] | ||
| + | [[Category: Li Y]] | ||
| + | [[Category: Murray DT]] | ||
Current revision
Cryo-EM Structure of a Tm1C Fibril
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