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  Crystal structure and mechanism of a DNA (6-4) photolyase

Maul, M. J., Barends, T., Glas, A. F., Cryle, M., Domratcheva, T., Schneider, S., et al. (2008). Crystal structure and mechanism of a DNA (6-4) photolyase. Angewandte Chemie International Edition: a journal of the Gesellschaft Deutscher Chemiker, 47(52), 10076-10080. doi:10.1002/anie.200804268.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0028-7993-8 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-DC23-1
Genre: Journal Article

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 Creators:
Maul, Melanie J., Author
Barends, Thomas1, Author           
Glas, Andreas F., Author
Cryle, Max1, Author           
Domratcheva, Tatiana1, Author           
Schneider, Sabine, Author
Schlichting, Ilme1, Author           
Carell, Thomas, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: DNA damage; DNA repair; enzymes; photochemistry; structure elucidation
 Abstract: UV irradiation of cells gives rise to the formation of cyclobutane pyrimidine dimers (CPD) and so-called (6-4) DNA lesions (Scheme 1). Both lesions are major photoproducts formed in dipyrimidine sequences of double-stranded DNA.1, 2 Repair of these lesions is essential because of their high mutagenic potential. Particularly important in many organisms are the photolyase-mediated repair systems that are able to split CPD lesions and (6-4) lesions directly back into their corresponding monomers.1, 2 While formation and photolyase repair of CPD lesions is well studied, little is known about (6-4) lesions. In particular, the mechanism of repair of the (6-4) lesions by (6-4) DNA photolyases is a long-standing question. Currently it is believed that the enzyme rearranges the (6-4) lesion with the help of two conserved histidine residues in the active site to form an oxetane intermediate (Scheme 1), which is split after single-electron donation from a light-activated FADH−.3, 4 We report here the first crystal structures of a (6-4) DNA photolyase enzyme. The structures show the enzyme in complex with a (6-4) lesion containing DNA before and after in situ repair. Based on the structural and biochemical data we propose a modified repair mechanism that lacks the strained oxetane intermediate.

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Language(s): eng - English
 Dates: 2008-08-292008-10-272008-10-272008-12-15
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.200804268
URI: http://www.ncbi.nlm.nih.gov/pubmed/18956392
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Title: Angewandte Chemie International Edition : a journal of the Gesellschaft Deutscher Chemiker
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 47 (52) Sequence Number: - Start / End Page: 10076 - 10080 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/110984073528720