1y66

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spinqualitylabelsall models 1y66, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant

Overview

Our goal was to compute a stable, full-sequence design of the Drosophila, melanogaster engrailed homeodomain. Thermal and chemical denaturation data, indicated the design was significantly more stable than was the wild-type, protein. The data were also nearly identical to those for a similar, later, full-sequence design, which was shown by NMR to adopt the homeodomain, fold: a three-helix, globular monomer. However, a 1.65 A crystal structure, of the design described here turned out to be of a completely different, fold: a four-helix, rodlike tetramer. The crystallization conditions, included approximately 25% dioxane, and subsequent experiments by circular, dichroism and sedimentation velocity analytical ultracentrifugation, indicated that dioxane increases the helicity and oligomerization state of, the designed protein. We attribute at least part of the discrepancy, between the target fold and the crystal structure to the presence of a, high concentration of dioxane.

About this Structure

1Y66 is a Protein complex structure of sequences from Escherichia coli with CD, DIO and ACY as ligands. Full crystallographic information is available from OCA.

Reference

Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant., Hom GK, Lassila JK, Thomas LM, Mayo SL, Protein Sci. 2005 Apr;14(4):1115-9. Epub 2005 Mar 1. PMID:15741348

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