Comparison of multiple crystal structures with NMR data for engrailed homeodomain |
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Authors: | Tomasz L Religa |
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Institution: | (1) MRC Centre for Protein Engineering, Hills Road, Cambridge, CB2 0QH, UK |
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Abstract: | Two methods are currently available to solve high resolution protein structures—X-ray crystallography and nuclear magnetic
resonance (NMR). Both methods usually produce highly similar structures, but small differences between both solutions are
always observed. Here the raw NMR data as well as the solved NMR structure were compared to the multiple crystal structures
solved for the WT 60 residue three helix bundle engrailed homeodomain (EnHD) and single point mutants. There was excellent
agreement between TALOS-predicted and crystal structure-observed dihedral angles and a good agreement for the 3
J(H
N
H
α
) couplings for the multiple crystal structures. Around 1% of NOEs were violated for any crystal structure, but no NOE was
inconsistent with all of the crystal structures. Violations usually occurred for surface residues or for residues for which
multiple discreet conformations were observed between the crystal structures. Comparison of the disorder shown in the multiple
crystal structures shows little correlation with dynamics under native conditions for this protein. |
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Keywords: | Backbone dynamics Crystallography Engrailed homeodomain NMR Side-chain dynamics Structure |
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