Tryptophan RNA-binding attenuation protein: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
TRAP is composed of 11 identical subunits arranged in a symmetrical ring. Tryptophan is bound to TRAP by mostly non-polar residues<ref>PMID:16698553</ref>.
TRAP is composed of 11 identical subunits arranged in a symmetrical ring. The <scene name='59/595823/Cv/2'>active site of TRAP</scene><ref>PMID:16698553</ref>.
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Revision as of 13:32, 30 March 2017


Function

Tryptophan RNA-binding attenuation protein (TRAP) is a tryptophan-activated RNA-binding protein which regulates the expression of the tryptophan biosynthesis genes. Down regulation of Trp biosynthesis is observed upon binding of 11 Trp to TRAP[1].

Structural highlights

TRAP is composed of 11 identical subunits arranged in a symmetrical ring. The [2].

Structure of tryptophan RNA-binding attenuation protein complex with Trp (PDB code 2exs).

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3D Structures of tryptophan RNA-binding attenuation protein3D Structures of tryptophan RNA-binding attenuation protein

Updated on 30-March-2017

ReferencesReferences

  1. Li PT, Gollnick P. Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity. J Mol Biol. 2004 Jan 16;335(3):707-22. PMID:14687568 doi:http://dx.doi.org/10.1016/S0022283603013846
  2. Heddle JG, Yokoyama T, Yamashita I, Park SY, Tame JR. Rounding up: Engineering 12-membered rings from the cyclic 11-mer TRAP. Structure. 2006 May;14(5):925-33. PMID:16698553 doi:http://dx.doi.org/10.1016/j.str.2006.03.013

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Michal Harel, Alexander Berchansky