1u8b

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|PDB= 1u8b |SIZE=350|CAPTION= <scene name='initialview01'>1u8b</scene>, resolution 2.10&Aring;
|PDB= 1u8b |SIZE=350|CAPTION= <scene name='initialview01'>1u8b</scene>, resolution 2.10&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= ADA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= ADA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u8b OCA], [http://www.ebi.ac.uk/pdbsum/1u8b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u8b RCSB]</span>
}}
}}
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[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
[[Category: Zhou, P.]]
[[Category: Zhou, P.]]
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[[Category: ZN]]
 
[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
[[Category: methylation]]
[[Category: methylation]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:28:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:41 2008''

Revision as of 21:06, 30 March 2008


PDB ID 1u8b

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , , , , , ,
Gene: ADA (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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