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5G33

Structure of Rad14 in complex with acetylnaphtyl-guanine containing DNA

Summary for 5G33
Entry DOI10.2210/pdb5g33/pdb
Related5G32 5G34 5G35
DescriptorRAD14, 5'-D(*GP*CP*TP*CP*TP*AP*MFOP*TP*CP*AP*TP*CP*AP*CP)-3', 5'-D(*GP*TP*GP*AP*TP*GP*AP*CP*GP*TP*AP*GP*AP*GP)-3', ... (5 entities in total)
Functional Keywordscell cycle, dna repair, nucleotide excision repair
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Total number of polymer chains6
Total formula weight49502.29
Authors
Simon, N.,Ebert, C.,Schneider, S. (deposition date: 2016-04-18, release date: 2016-06-01, Last modification date: 2024-01-10)
Primary citationSchneider, S.,Simon, N.,Ebert, C.
Structural Basis for Bulky Adduct DNA Lesion Recognition by the Nucleotide Excision Repair Protein Rad14.
Chemistry, 22:10782-, 2016
Cited by
PubMed Abstract: Heterocyclic aromatic amines react with purine bases and result in bulky DNA adducts that cause mutations. Such structurally diverse lesions are substrates for the nucleotide excision repair (NER). It is thought that the NER machinery recognises and verifies distorted DNA conformations, also involving the xeroderma pigmentosum group A and C proteins (XPA, XPC) that act as a scaffold between the DNA substrate and several other NER proteins. Here we present the synthesis of DNA molecules containing the polycyclic, aromatic amine C8-guanine lesions acetylaminophenyl, acetylaminonaphthyl, acetylaminoanthryl, and acetylaminopyrenyl, as well as their crystal structures in complex with the yeast XPA homologue Rad14. This work further substantiates the indirect lesion-detection mechanism employed by the NER system that recognises destabilised and deformable DNA structures.
PubMed: 27223336
DOI: 10.1002/CHEM.201602438
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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