2W35 : Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair
Description
Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.15 Classification:HYDROLASE Release Date:2009-01-20 Deposition Date:2008-11-06 Revision Date:2011-05-08#2011-07-13 Molecular Weight:60470.57 Macromolecule Type:Protein#DNA Residue Count:480 Atom Site Count:4015 DOI:10.2210/pdb2w35/pdb Abstract: Endonuclease V (EndoV) initiates a major base-repair pathway for nitrosative deamination resulting from endogenous processes and increased by oxidative stress from mitochondrial dysfunction or inflammatory responses. We solved the crystal structures of Thermotoga maritima EndoV in complex with a hypoxanthine lesion substrate and with product DNA. The PYIP wedge motif acts as a minor groove-damage sensor for helical distortions and base mismatches and separates DNA strands at the lesion. EndoV incises DNA with an unusual offset nick 1 nucleotide 3' of the lesion, as the deaminated adenine is rotated approximately 90 degrees into a recognition pocket approximately 8 A from the catalytic site. Tight binding by the lesion-recognition pocket in addition to Mg(2+) and hydrogen-bonding interactions to the DNA ends stabilize the product complex, suggesting an orderly recruitment of downstream proteins in this base-repair pathway.
Publication Date
1-20-2009
Publisher
RCSB-PDB
DOI
10.2210/pdb2w35/pdb
Document Type
Data Set
Recommended Citation
Dalhus, Bjørn; Rosnes, Ida; Alseth, Ingrun; Gao, Honghai; Cao, Weiguo; Bjørås, Magnar; Tainer, John A.; Backe, Paul H.; Arvai, Andrew S. (2009), "2W35 : Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair", RCSB-PDB, doi: 10.2210/pdb2w35/pdb
https://doi.org/10.2210/pdb2w35/pdb
Identifier
2W35
Embargo Date
1-20-2009