9C1U

Cryo-EM Structure of a Tm1C Fibril

Summary for 9C1U

• Entry DOI: 10.2210/pdb9c1u/pdb
• EMDB information: 45130
• Descriptor: Tropomyosin 1 I/C (1 entity in total)
• Functional Keywords: protein fibril
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 12
• Total formula weight: 89046.42

Authors

Fonda, B.D.,Kato, M.,Li, Y.,Murray, D.T. (deposition date: 2024-05-29, release date: 2024-10-09)

Primary citation

Fonda, B.D.,Kato, M.,Li, Y.,Murray, D.T.
Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils.
Protein Sci., 33:e5168-e5168, 2024

PubMed Abstract: 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.

PubMed: 39276003
DOI: 10.1002/pro.5168

Experimental method

ELECTRON MICROSCOPY (2.31 Å)