1tjl

From Proteopedia

Revision as of 01:12, 21 November 2007

Crystal structure of transcription factor DksA from E. coli

Overview

Bacterial transcription is regulated by the alarmone ppGpp, which binds, near the catalytic site of RNA polymerase (RNAP) and modulates its, activity. We show that the DksA protein is a crucial component of, ppGpp-dependent regulation. The 2.0 A resolution structure of Escherichia, coli DksA reveals a globular domain and a coiled coil with two highly, conserved Asp residues at its tip that is reminiscent of the transcript, cleavage factor GreA. This structural similarity suggests that DksA coiled, coil protrudes into the RNAP secondary channel to coordinate a ppGpp bound, Mg2+ ion with the Asp residues, thereby stabilizing the ppGpp-RNAP, complex. Biochemical analysis demonstrates that DksA affects transcript, elongation, albeit differently from GreA; augments ppGpp effects on, initiation; and binds directly to RNAP, positioning the Asp residues near, the active site. Substitution of these residues eliminates the synergy, between DksA and ppGpp. Thus, the secondary channel emerges as a common, regulatory entrance for transcription factors.

About this Structure

1TJL is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Regulation through the secondary channel--structural framework for ppGpp-DksA synergism during transcription., Perederina A, Svetlov V, Vassylyeva MN, Tahirov TH, Yokoyama S, Artsimovitch I, Vassylyev DG, Cell. 2004 Aug 6;118(3):297-309. PMID:15294156

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