1utd

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1utd, resolution 2.10Å

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THE STRUCTURE OF THE TRP RAN-BINDING ATTENUATION PROTEIN (TRAP) BOUND TO A 63-NUCLEOTIDE RNA MOLECULE CONTAINING GAGUUU REPEATS

Overview

The trp RNA-binding attenuation protein (TRAP) regulates expression of the, tryptophan biosynthetic genes in several Bacilli by binding to the leader, region of the nascent trp mRNA, inhibiting continued transcription. The 11, subunit TRAP molecule is active in complex with tryptophan, and binds, consequently an RNA target segment consisting of 11 (G/U)AG triplets, each, separated by two or three non-conserved "spacer" nucleotides. Here, we, report the first crystal structures of TRAP in a complex with RNA, containing UAG triplets separated by two nucleotides and in a complex with, RNA containing GAG triplets separated by three nucleotides. Comparison, with known structures of TRAP-RNA complexes shows that both substitution, of G-1 with U-1 in the triplet and addition of an extra spacer ... [(full description)]

About this Structure

1UTD is a [Single protein] structure of sequence from [Bacillus stearothermophilus] with TRP as [ligand]. Full crystallographic information is available from [OCA].

Reference

The interaction of RNA with TRAP: the role of triplet repeats and separating spacer nucleotides., Hopcroft NH, Manfredo A, Wendt AL, Brzozowski AM, Gollnick P, Antson AA, J Mol Biol. 2004 Apr 16;338(1):43-53. PMID:15050822

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