1ZGW

NMR structure of E. Coli Ada protein in complex with DNA

Summary for 1ZGW

• Entry DOI: 10.2210/pdb1zgw/pdb
• Related: 1ADN 1U8B
• Descriptor: 5'-D(*GP*CP*AP*AP*AP*TP*TP*AP*AP*AP*GP*CP*GP*CP*AP*AP*GP*A)-3', 5'-D(*TP*CP*TP*TP*GP*CP*GP*CP*TP*TP*TP*AP*AP*TP*TP*TP*GP*C)-3', Ada polyprotein, ... (4 entities in total)
• Functional Keywords: protein-dna complex, helix-turn-helix, zinc ligand, transcription regulator-dna complex, transcription regulator/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 27002.89

Authors

He, C.,Hus, J.C.,Sun, L.J.,Zhou, P.,Norman, D.P.,Doetsch, V.,Wei, H.,Gross, J.D.,Lane, W.S.,Wagner, G.,Verdine, G.L. (deposition date: 2005-04-22, release date: 2005-10-18, Last modification date: 2024-11-06)

Primary citation

He, C.,Hus, J.C.,Sun, L.J.,Zhou, P.,Norman, D.P.,Doetsch, 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

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

Experimental method

SOLUTION NMR