1aoy

From Proteopedia

Revision as of 07:32, 2 May 2008 by OCA (Talk | contribs)
Jump to: navigation, search

Template:STRUCTURE 1aoy

N-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR NMR, 23 STRUCTURES


Overview

The structure of the monomeric DNA-binding domain of the Escherichia coli arginine repressor, ArgR, determined by NMR spectroscopy, shows structural homology to the winged helix-turn-helix (wHTH) family, a motif found in a diverse class of proteins including both gene regulators and gene organizers from prokaryotes and eukaryotes. Biochemical data on DNA binding by intact ArgR are used as constraints to position the domain on its DNA target and to derive a model for the hexamer-DNA complex using the known structure of the L-arginine-binding domain. The structural independence of the wHTH fold may be important for multimeric DNA-binding proteins that contact extended DNA regions with imperfect match to consensus sequences, a feature of many wHTH-domain proteins.

About this Structure

1AOY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA., Sunnerhagen M, Nilges M, Otting G, Carey J, Nat Struct Biol. 1997 Oct;4(10):819-26. PMID:9334747 Page seeded by OCA on Fri May 2 10:32:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools