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1U8B

Crystal structure of the methylated N-ADA/DNA complex

Summary for 1U8B
Entry DOI10.2210/pdb1u8b/pdb
Descriptor5'-D(*TP*AP*AP*AP*TP*T)-3', 5'-D(P*AP*AP*TP*TP*T)-3', 5'-D(P*AP*AP*AP*GP*CP*GP*CP*AP*AP*GP*AP*T)-3', ... (7 entities in total)
Functional Keywordsprotein-dna complex, methylation, zinc, helix-turn-helix, metal binding protein-dna complex, metal binding protein/dna
Biological sourceEscherichia coli
Total number of polymer chains5
Total formula weight26432.91
Authors
He, C.,Hus, J.-C.,Sun, L.J.,Zhou, P.,Norman, D.P.G.,Dotsch, V.,Gross, J.D.,Lane, W.S.,Wagner, G.,Verdine, G.L. (deposition date: 2004-08-05, release date: 2005-10-11, Last modification date: 2024-11-06)
Primary citationHe, C.,Hus, J.C.,Sun, L.J.,Zhou, P.,Norman, D.P.,Dotsch, V.,Wei, H.,Gross, J.D.,Lane, W.S.,Wagner, G.,Verdine, G.L.
A methylation-dependent electrostatic switch controls DNA repair and transcriptional activation by E. coli ada.
Mol.Cell, 20:117-129, 2005
Cited by
PubMed Abstract: 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.
PubMed: 16209950
DOI: 10.1016/j.molcel.2005.08.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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