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2W35

Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair

Summary for 2W35
Entry DOI10.2210/pdb2w35/pdb
Related2W36
DescriptorEndonuclease V, 5'-D(*AP*TP*GP*CP*GP*AP*CP*IP*GP)-3', 5'-D(*AP*GP*CP*CP*GP*TP)-3', ... (5 entities in total)
Functional Keywordshypoxanthine, endonuclease, endonucleasev, hydrolase, inosine, dna damage, dna repair
Biological sourceThermotoga maritima
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Cellular locationCytoplasm (By similarity): Q9X2H9
Total number of polymer chains6
Total formula weight60470.57
Authors
Dalhus, B.,Arvai, A.S.,Rosnes, I.,Olsen, O.E.,Backe, P.H.,Alseth, I.,Gao, H.,Cao, W.,Tainer, J.A.,Bjoras, M. (deposition date: 2008-11-06, release date: 2009-01-20, Last modification date: 2024-06-19)
Primary citationDalhus, B.,Arvai, A.S.,Rosnes, I.,Olsen, O.E.,Backe, P.H.,Alseth, I.,Gao, H.,Cao, W.,Tainer, J.A.,Bjoras, M.
Structures of Endonuclease V with DNA Reveal Initiation of Deaminated Adenine Repair.
Nat.Struct.Mol.Biol., 16:138-, 2009
Cited by
PubMed 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.
PubMed: 19136958
DOI: 10.1038/NSMB.1538
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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