1u8b
From Proteopedia
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Crystal structure of the methylated N-ADA/DNA complex
Overview
The transcriptional activity of many sequence-specific DNA binding, proteins is directly regulated by posttranslational covalent modification., Although this form of regulation was first described nearly two decades, ago, it remains poorly understood at a mechanistic level. The prototype, for a transcription factor controlled by posttranslational modification is, E. coli Ada protein, a chemosensor that both repairs methylation damage in, DNA and coordinates the resistance response to genotoxic methylating, agents. Ada repairs methyl phosphotriester lesions in DNA by transferring, the aberrant methyl group to one of its own cysteine residues; this, site-specific methylation enhances tremendously the DNA binding activity, of the protein, thereby enabling it to activate a methylation-resistance, regulon. Here, we report solution and X-ray structures of the, Cys-methylated chemosensor domain of Ada bound to DNA. The structures, reveal that both phosphotriester repair and methylation-dependent, transcriptional activation function through a zinc- and, methylation-dependent electrostatic switch.
About this Structure
1U8B is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada., He C, Hus JC, Sun LJ, Zhou P, Norman DP, Dotsch V, Wei H, Gross JD, Lane WS, Wagner G, Verdine GL, Mol Cell. 2005 Oct 7;20(1):117-29. PMID:16209950
Page seeded by OCA on Wed Nov 21 03:55:19 2007
Categories: Escherichia coli | Single protein | Dotsch, V. | Gross, J.D. | He, C. | Hus, J.C. | Lane, W.S. | Norman, D.P.G. | Sun, L.J. | Verdine, G.L. | Wagner, G. | Zhou, P. | ZN | Helix-turn-helix | Methylation | Protein-dna complex | Zinc
