Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution

Vladimir A Meshcheryakov; Inna Krieger; Alla S Kostyukova; Fadel A Samatey

doi:10.1107/S090744491102645X

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Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution

Journal article

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Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution

Vladimir A Meshcheryakov, Inna Krieger, Alla S Kostyukova and Fadel A Samatey

Acta crystallographica. Section D, Biological crystallography., Vol.67(Pt 9), pp.822-825

09/01/2011

DOI: https://doi.org/10.1107/S090744491102645X

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https://hdl.handle.net/2376/110301

PMCID: PMC3169316

PMID: 21904035

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Abstract

coiled coils

tropomodulin-binding proteins

Research Papers

cytoskeletal proteins

actin-binding proteins

The crystal structure of the N-terminal fragment of the short nonmuscle α-tropomyosin has been determined at a resolution of 0.98 Å. Tropomyosin (TM) is an elongated two-chain protein that binds along actin filaments. Important binding sites are localized in the N-terminus of tropomyosin. The structure of the N-terminus of the long muscle α-TM has been solved by both NMR and X-ray crystallography. Only the NMR structure of the N-terminus of the short nonmuscle α-TM is available. Here, the crystal structure of the N-terminus of the short nonmuscle α-TM (αTm1bZip) at a resolution of 0.98 Å is reported, which was solved from crystals belonging to space group P 3 1 with unit-cell parameters a = b = 33.00, c = 52.03 Å, α = β = 90, γ = 120°. The first five N-terminal residues are flexible and residues 6–35 form an α-helical coiled coil. The overall fold and the secondary structure of the crystal structure of αTM1bZip are highly similar to the NMR structure and the atomic coordinates of the corresponding C α atoms between the two structures superimpose with a root-mean-square deviation of 0.60 Å. The crystal structure validates the NMR structure, with the positions of the side chains being determined precisely in our structure.

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Title: Structure of a tropomyosin N-terminal fragment at 0.98 Å resolution
Creators: Vladimir A Meshcheryakov - Trans-Membrane Trafficking Unit
Inna Krieger - Department of Biochemistry and Biophysics
Alla S Kostyukova - Department of Neuroscience and Cell Biology
Fadel A Samatey - Trans-Membrane Trafficking Unit
Publication Details: Acta crystallographica. Section D, Biological crystallography., Vol.67(Pt 9), pp.822-825
Academic Unit: Chemical Engineering and Bioengineering, School of
Publisher: International Union of Crystallography
Identifiers: 99900547150201842
Language: English
Resource Type: Journal article