7f8t: Difference between revisions
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==Re-refinement of the 2XRY X-ray structure of archaeal class II CPD photolyase from Methanosarcina mazei== | ==Re-refinement of the 2XRY X-ray structure of archaeal class II CPD photolyase from Methanosarcina mazei== | ||
<StructureSection load='7f8t' size='340' side='right'caption='[[7f8t]]' scene=''> | <StructureSection load='7f8t' size='340' side='right'caption='[[7f8t]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F8T FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f8t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F8T FirstGlance]. <br> | ||
</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=7f8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f8t OCA], [https://pdbe.org/7f8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f8t RCSB], [https://www.ebi.ac.uk/pdbsum/7f8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f8t ProSAT]</span></td></tr> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xry|2xry]]</div></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=7f8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f8t OCA], [https://pdbe.org/7f8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f8t RCSB], [https://www.ebi.ac.uk/pdbsum/7f8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f8t ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7f8t" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bessho Y]] | [[Category: Bessho, Y]] | ||
[[Category: Chang Y | [[Category: Chang, Y K]] | ||
[[Category: Essen L | [[Category: Essen, L O]] | ||
[[Category: Franz-Badur S]] | [[Category: Franz-Badur, S]] | ||
[[Category: Gusti-Ngurah-Putu E | [[Category: Gusti-Ngurah-Putu, E P]] | ||
[[Category: Huang K | [[Category: Huang, K F]] | ||
[[Category: Huang | [[Category: Huang, W C]] | ||
[[Category: Iwata S]] | [[Category: Iwata, S]] | ||
[[Category: Joti Y]] | [[Category: Joti, Y]] | ||
[[Category: Kiontke S]] | [[Category: Kiontke, S]] | ||
[[Category: Lee C | [[Category: Lee, C C]] | ||
[[Category: Liao J | [[Category: Liao, J H]] | ||
[[Category: Maestre-Reyna M]] | [[Category: Maestre-Reyna, M]] | ||
[[Category: Nango E]] | [[Category: Nango, E]] | ||
[[Category: Owada S]] | [[Category: Owada, S]] | ||
[[Category: Sugahara M]] | [[Category: Sugahara, M]] | ||
[[Category: Tanaka R]] | [[Category: Tanaka, R]] | ||
[[Category: Tono K]] | [[Category: Tono, K]] | ||
[[Category: Tsai M | [[Category: Tsai, M D]] | ||
[[Category: Wang P | [[Category: Wang, P H]] | ||
[[Category: Weng J | [[Category: Weng, J H]] | ||
[[Category: Wu H | [[Category: Wu, H Y]] | ||
[[Category: Wu W | [[Category: Wu, W J]] | ||
[[Category: Yamamoto J]] | [[Category: Yamamoto, J]] | ||
[[Category: Yang C | [[Category: Yang, C H]] | ||
[[Category: Dna binding protein]] | |||
[[Category: Lyase]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Photoreduction]] | |||
[[Category: Redox state]] | |||
