1lea
From Proteopedia
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SOLUTION STRUCTURE OF THE LEXA REPRESSOR DNA BINDING DETERMINED BY 1H NMR SPECTROSCOPY
Overview
The structure of the 84 residue DNA binding domain of the Escherichia coli, LexA repressor has been determined from NMR data using distance geometry, and restrained molecular dynamics. The assignment of the 1H NMR spectrum, of the molecule, derived from 2- and 3-D homonuclear experiments, is also, reported. A total of 613 non-redundant distance restraints were used to, give a final family of 28 structures. The structured region of the, molecule consisted of residues 4-69 and yielded a r.m.s. deviation from an, average of 0.9 A for backbone and 1.6 A for all heavy atoms. The structure, contains three regular alpha-helices at residues 6-21 (I), 28-35 (II) and, 41-52 (III), and an antiparallel beta-sheet at residues 56-58 and 66-68., Helices II and III form a variant helix-turn-helix DNA binding motif, with, an unusual one residue insert at residue 38. The topology of the LexA DNA, binding domain is found to be the same as for the DNA binding domains of, the catabolic activator protein, human histone 5, the HNF-3/fork head, protein and the Kluyveromyces lactis heat shock transcription factor.
About this Structure
1LEA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy., Fogh RH, Ottleben G, Ruterjans H, Schnarr M, Boelens R, Kaptein R, EMBO J. 1994 Sep 1;13(17):3936-44. PMID:8076591
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