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| | <StructureSection load='2xry' size='340' side='right'caption='[[2xry]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='2xry' size='340' side='right'caption='[[2xry]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xry]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Metma Metma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei_Go1 Methanosarcina mazei Go1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XRY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xrz|2xrz]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribodipyrimidine_photo-lyase Deoxyribodipyrimidine photo-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.3 4.1.99.3] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xry OCA], [https://pdbe.org/2xry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xry RCSB], [https://www.ebi.ac.uk/pdbsum/2xry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xry ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xry OCA], [http://pdbe.org/2xry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xry RCSB], [http://www.ebi.ac.uk/pdbsum/2xry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xry ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q8PYK9_METMA Q8PYK9_METMA] |
| - | 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>
| + | |
| - | <div class="pdbe-citations 2xry" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Deoxyribodipyrimidine photo-lyase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metma]] | + | [[Category: Methanosarcina mazei Go1]] |
| - | [[Category: Batschauer, A]] | + | [[Category: Batschauer A]] |
| - | [[Category: Carell, T]] | + | [[Category: Carell T]] |
| - | [[Category: Essen, L O]] | + | [[Category: Essen LO]] |
| - | [[Category: Geisselbrecht, Y]] | + | [[Category: Geisselbrecht Y]] |
| - | [[Category: Kiontke, S]] | + | [[Category: Kiontke S]] |
| - | [[Category: Pokorny, R]] | + | [[Category: Pokorny R]] |
| - | [[Category: Dna damage]]
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| - | [[Category: Dna repair]]
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| - | [[Category: Lyase]]
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