9c1u
From Proteopedia
Cryo-EM Structure of a Tm1C Fibril
Structural highlights
FunctionQ95TA3_DROME Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.[ARBA:ARBA00002987] Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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