2JWT

Solution structure of Engrailed homeodomain WT

Summary for 2JWT

• Entry DOI: 10.2210/pdb2jwt/pdb
• Related: 1ENH
• NMR Information: BMRB: 15536
• Descriptor: Segmentation polarity homeobox protein engrailed (1 entity in total)
• Functional Keywords: homeodomain, developmental protein, dna-binding, homeobox, nucleus, phosphorylation, repressor, segmentation polarity protein, transcription, transcription regulation
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 7469.55

Authors

Religa, T.L. (deposition date: 2007-10-24, release date: 2008-04-01, Last modification date: 2024-05-08)

Primary citation

Religa, T.L.
Comparison of multiple crystal structures with NMR data for engrailed homeodomain
J.Biomol.Nmr, 40:189-202, 2008

PubMed 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 ( alpha )) 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.

PubMed: 18274703
DOI: 10.1007/s10858-008-9223-9

Experimental method

SOLUTION NMR