5g33

Structure of Rad14 in complex with acetylnaphtyl-guanine containing DNA

spinqualitylabelsall models 5g33, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g33 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 2.4Å Ligands: MFO, ZN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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