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7ZTD

Non-muscle F-actin decorated with non-muscle tropomyosin 3.2

Summary for 7ZTD
Entry DOI10.2210/pdb7ztd/pdb
EMDB information14958
Descriptoractin, cytoplasmic 1, Non-muscle tropomyosin 3.2, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordsactin, tropomyosin, non-muscle, complex, cytosolic protein
Biological sourceHomo sapiens
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Total number of polymer chains12
Total formula weight383707.59
Authors
Selvaraj, M.,Kokate, S.,Kogan, K.,Kotila, T.,Kremneva, E.,Lappalainen, P.,Huiskonen, J.T. (deposition date: 2022-05-09, release date: 2023-01-11, Last modification date: 2024-07-24)
Primary citationSelvaraj, M.,Kokate, S.B.,Reggiano, G.,Kogan, K.,Kotila, T.,Kremneva, E.,DiMaio, F.,Lappalainen, P.,Huiskonen, J.T.
Structural basis underlying specific biochemical activities of non-muscle tropomyosin isoforms.
Cell Rep, 42:111900-111900, 2023
Cited by
PubMed Abstract: The actin cytoskeleton is critical for cell migration, morphogenesis, endocytosis, organelle dynamics, and cytokinesis. To support diverse cellular processes, actin filaments form a variety of structures with specific architectures and dynamic properties. Key proteins specifying actin filaments are tropomyosins. Non-muscle cells express several functionally non-redundant tropomyosin isoforms, which differentially control the interactions of other proteins, including myosins and ADF/cofilin, with actin filaments. However, the underlying molecular mechanisms have remained elusive. By determining the cryogenic electron microscopy structures of actin filaments decorated by two functionally distinct non-muscle tropomyosin isoforms, Tpm1.6 and Tpm3.2, we reveal that actin filament conformation remains unaffected upon binding. However, Tpm1.6 and Tpm3.2 follow different paths along the actin filament major groove, providing an explanation for their incapability to co-polymerize on actin filaments. We also elucidate the molecular basis underlying specific roles of Tpm1.6 and Tpm3.2 in myosin II activation and protecting actin filaments from ADF/cofilin-catalyzed severing.
PubMed: 36586407
DOI: 10.1016/j.celrep.2022.111900
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.6 Å)
Structure validation

226707

數據於2024-10-30公開中

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