3azd
From Proteopedia
Crystal structure of tropomyosin N-terminal fragment at 0.98A resolution
Structural highlights
FunctionGCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. Publication Abstract from PubMedTropomyosin (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 alpha-TM has been solved by both NMR and X-ray crystallography. Only the NMR structure of the N-terminus of the short nonmuscle alpha-TM is available. Here, the crystal structure of the N-terminus of the short nonmuscle alpha-TM (alphaTm1bZip) at a resolution of 0.98 A is reported, which was solved from crystals belonging to space group P3(1) with unit-cell parameters a = b = 33.00, c = 52.03 A, alpha = beta = 90, gamma = 120 degrees . The first five N-terminal residues are flexible and residues 6-35 form an alpha-helical coiled coil. The overall fold and the secondary structure of the crystal structure of alphaTM1bZip are highly similar to the NMR structure and the atomic coordinates of the corresponding C(alpha) atoms between the two structures superimpose with a root-mean-square deviation of 0.60 A. The crystal structure validates the NMR structure, with the positions of the side chains being determined precisely in our structure. Structure of a tropomyosin N-terminal fragment at 0.98 A resolution.,Meshcheryakov VA, Krieger I, Kostyukova AS, Samatey FA Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):822-5. Epub 2011, Aug 9. PMID:21904035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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