5g32

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Structure of Rad14 in complex with acetylaminophenyl-guanine containing DNAStructure of Rad14 in complex with acetylaminophenyl-guanine containing DNA

Structural highlights

5g32 is a 6 chain structure with sequence from Saccharomyces cerevisiae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RAD14_YEAST Involved in nucleotide excision repair. Binds specifically to damaged DNA. Required for the incision step.

Publication Abstract from PubMed

Heterocyclic aromatic amines react with purine bases and result in bulky DNA adducts which cause mutations. Such structurally diverse lesions are substrates for the nucleotide excision repair (NER). It is thought that the NER machinery recognises distorted DNA conformations, involving the xeroderma pigmentosum group A and C (XPA, XPC) proteins as a scaffold between the DNA substrate and several other NER proteins. Here we present the synthesis of DNA containing the polycyclic aromatic amine C8-guanine lesions acetylaminophenyl, acetylaminonaphthyl, acetylaminoanthryl and acetylaminopyrenyl as well as their crystal structures in in complex with the yeast XPA homologue Rad14. This work further substantiates the indirect lesion detection mechanism employed by the NER system to recognise destabilised and deformable DNA structures.

Structural basis for bulky adduct DNA lesion recognition by the nucleotide excision repair protein Rad14.,Schneider S, Simon N, Ebert C Chemistry. 2016 May 25. doi: 10.1002/chem.201602438. PMID:27223336[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Schneider S, Simon N, Ebert C. Structural basis for bulky adduct DNA lesion recognition by the nucleotide excision repair protein Rad14. Chemistry. 2016 May 25. doi: 10.1002/chem.201602438. PMID:27223336 doi:http://dx.doi.org/10.1002/chem.201602438

5g32, resolution 2.20Å

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