5G33

Structure of Rad14 in complex with acetylnaphtyl-guanine containing DNA

Summary for 5G33

• Entry DOI: 10.2210/pdb5g33/pdb
• Related: 5G32 5G34 5G35
• Descriptor: RAD14, 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 Keywords: cell cycle, dna repair, nucleotide excision repair
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 6
• Total formula weight: 49502.29

Authors

Simon, N.,Ebert, C.,Schneider, S. (deposition date: 2016-04-18, release date: 2016-06-01, Last modification date: 2024-01-10)

Primary citation

Schneider, S.,Simon, N.,Ebert, C.
Structural Basis for Bulky Adduct DNA Lesion Recognition by the Nucleotide Excision Repair Protein Rad14.
Chemistry, 22:10782-, 2016

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)