1adr
From Proteopedia
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DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE DNA-BINDING DOMAIN OF THE P22 C2 REPRESSOR (1-76) IN SOLUTION AND COMPARISON WITH THE DNA-BINDING DOMAIN OF THE 434 REPRESSOR
Overview
The solution structure of the N-terminal DNA-binding domain of the P22 c2, repressor (residues 1 to 76) was determined by nuclear magnetic resonance, (NMR) spectroscopy. The structure determination was based on nearly, complete sequence-specific resonance assignments for 1H, 13C and 15N, and, tables of the chemical shifts for all three nuclei are included here. A, group of 20 conformers was calculated from the NMR constraints using the, program DIANA, and energy-minimized using an implementation of the AMBER, force field in the program OPAL. The core of the protein formed by, residues 5 to 68 is structurally well defined, with an average of 0.7 A, for the root-mean-square deviations calculated for the backbone atoms of, the individual conformers relative to the mean coordinates. The N-terminal, tetrapeptide segment and the C-terminal octapeptide segment are flexibly, disordered. The molecular architecture includes five alpha-helical, segments with residues 6 to 17, 21 to 28, 32 to 39, 47 to 57 and 61 to 65., The length and relative orientation of these helices are closely similar, to the arrangement of corresponding regular secondary structures in the, DNA-binding domain of the 434 repressor, with the sole exception of the, fourth helix, which is one turn longer at its amino-terminal end than the, corresponding helix in the 434 repressor. This extension of the fourth, helix implies that the DNA-binding mode of the P22 c2 repressor must be, somewhat different from that observed for the 434 repressor. Exact, superposition of two P22 c2 repressor DNA-binding domains for best fit of, corresponding polypeptide backbone atoms onto the two 434 repressor, DNA-binding domains in the crystal structure of the 434 repressor-DNA, complex would result in a model of the P22 c2 repressor-DNA complex which, could not accommodate the fourth helices because of steric overlap.
About this Structure
1ADR is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor., Sevilla-Sierra P, Otting G, Wuthrich K, J Mol Biol. 1994 Jan 21;235(3):1003-20. PMID:8289306
Page seeded by OCA on Tue Nov 20 10:46:50 2007
