1o7l
From Proteopedia
|
MOLYBDATE-ACTIVATED FORM OF MODE FROM ESCHERICHIA COLI
Overview
ModE is a bacterial transcriptional regulator that orchestrates many, aspects of molybdenum metabolism by binding to specific DNA sequences in a, molybdate-dependent fashion. We present the crystal structure of, Escherichia coli ModE in complex with molybdate, which was determined at, 2.75A from a merohedrally twinned crystal (twin fraction approximately, 0.30) with space group P4(3). We now have structures of ModE in both its, "switched on" (ligand-bound) and "switched off" (apo) states. Comparison, with the apo structure shows that ligand binding leads to extensive, conformational changes not only in the molybdate-binding domain, but also, in the DNA-binding domain. The most obvious difference is the loss of the, pronounced asymmetry between the two chains of the ModE dimer, which had, been a characteristic property of the apo structure. Another major change, concerns the relative orientation of the two DNA-interacting winged, helix-turn-helix motifs. Manual docking of an idealized DNA structure, suggests that this conformational change should improve DNA binding of the, activated molybdate-bound ModE.
About this Structure
1O7L is a Single protein structure of sequence from Escherichia coli with CL, CA and MOO as ligands. Structure known Active Site: MO1. Full crystallographic information is available from OCA.
Reference
Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains., Schuttelkopf AW, Boxer DH, Hunter WN, J Mol Biol. 2003 Feb 21;326(3):761-7. PMID:12581638
Page seeded by OCA on Mon Nov 5 16:45:40 2007
