UV damage endonuclease employs a novel dual-dinucleotide flipping mechanism to recognize different DNA lesions

Repairing damaged DNA is essential for an organism's survival. UV damage endonuclease (UVDE) is a DNA-repair enzyme that can recognize and incise different types of damaged DNA. We present the structure of Sulfolobus acidocaldarius UVDE on its own and in a pre-catalytic complex with UV-damaged...

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Published inNucleic acids research Vol. 41; no. 2; pp. 1363 - 1371
Main Authors Meulenbroek, Elisabeth M, Peron Cane, Caroline, Jala, Isabelle, Iwai, Shigenori, Moolenaar, Geri F, Goosen, Nora, Pannu, Navraj S
Format Journal Article
LanguageEnglish
Published England Oxford University Press 01.01.2013
Subjects
Amino Acid Sequence
DNA
DNA - chemistry
DNA Damage
DNA Repair Enzymes - chemistry
DNA Repair Enzymes - metabolism
Endodeoxyribonucleases - chemistry
Endodeoxyribonucleases - metabolism
Endonuclease
Enzymes
Metals - chemistry
Models, Molecular
Molecular Sequence Data
purines
Pyrimidine Dimers - metabolism
pyrimidines
Sequence Alignment
Structural Biology
Sulfolobus acidocaldarius
Sulfolobus acidocaldarius - enzymology
Survival
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Summary:Repairing damaged DNA is essential for an organism's survival. UV damage endonuclease (UVDE) is a DNA-repair enzyme that can recognize and incise different types of damaged DNA. We present the structure of Sulfolobus acidocaldarius UVDE on its own and in a pre-catalytic complex with UV-damaged DNA containing a 6-4 photoproduct showing a novel 'dual dinucleotide flip' mechanism for recognition of damaged dipyrimidines: the two purines opposite to the damaged pyrimidine bases are flipped into a dipurine-specific pocket, while the damaged bases are also flipped into another cleft.
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ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gks1127