3AZD

Crystal structure of tropomyosin N-terminal fragment at 0.98A resolution

Summary for 3AZD

• Entry DOI: 10.2210/pdb3azd/pdb
• Descriptor: short alpha-tropomyosin,transcription factor GCN4 (2 entities in total)
• Functional Keywords: coiled-coil, actin-binding protein, muscle protein
• Biological source: Rattus norvegicus (Rat); More
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 2
• Total formula weight: 8549.73

Authors

Meshcheryakov, V.A.,Krieger, I.,Kostyukova, A.S.,Samatey, F.A. (deposition date: 2011-05-23, release date: 2011-10-19, Last modification date: 2023-11-01)

Primary citation

Meshcheryakov, V.A.,Krieger, I.,Kostyukova, A.S.,Samatey, F.A.
Structure of a tropomyosin N-terminal fragment at 0.98 A resolution
Acta Crystallogr.,Sect.D, 67:822-825, 2011

PubMed Abstract: 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 P3(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.

PubMed: 21904035
DOI: 10.1107/S090744491102645X

Experimental method

X-RAY DIFFRACTION (0.98 Å)