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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q8PYK9_METMA Q8PYK9_METMA] | | [https://www.uniprot.org/uniprot/Q8PYK9_METMA Q8PYK9_METMA] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Class II photolyases ubiquitously occur in plants, animals, prokaryotes and some viruses. Like the distantly related microbial class I photolyases, these enzymes repair UV-induced cyclobutane pyrimidine dimer (CPD) lesions within duplex DNA using blue/near-UV light. Methanosarcina mazei Mm0852 is a class II photolyase of the archaeal order of Methanosarcinales, and is closely related to plant and metazoan counterparts. Mm0852 catalyses light-driven DNA repair and photoreduction, but in contrast to class I enzymes lacks a high degree of binding discrimination between UV-damaged and intact duplex DNA. We solved crystal structures of Mm0852, the first one for a class II photolyase, alone and in complex with CPD lesion-containing duplex DNA. The lesion-binding mode differs from other photolyases by a larger DNA-binding site, and an unrepaired CPD lesion is found flipped into the active site and recognized by a cluster of five water molecules next to the bound 3'-thymine base. Different from other members of the photolyase-cryptochrome family, class II photolyases appear to utilize an unusual, conserved tryptophane dyad as electron transfer pathway to the catalytic FAD cofactor.
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| Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA.,Kiontke S, Geisselbrecht Y, Pokorny R, Carell T, Batschauer A, Essen LO EMBO J. 2011 Sep 2. doi: 10.1038/emboj.2011.313. PMID:21892138<ref>PMID:21892138</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2xry" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
