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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]] | |||
Revision as of 06:04, 21 April 2022
Re-refinement of the 2XRY X-ray structure of archaeal class II CPD photolyase from Methanosarcina mazeiRe-refinement of the 2XRY X-ray structure of archaeal class II CPD photolyase from Methanosarcina mazei
Structural highlights
Publication Abstract from PubMedClass 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Large Structures
- Bessho, Y
- Chang, Y K
- Essen, L O
- Franz-Badur, S
- Gusti-Ngurah-Putu, E P
- Huang, K F
- Huang, W C
- Iwata, S
- Joti, Y
- Kiontke, S
- Lee, C C
- Liao, J H
- Maestre-Reyna, M
- Nango, E
- Owada, S
- Sugahara, M
- Tanaka, R
- Tono, K
- Tsai, M D
- Wang, P H
- Weng, J H
- Wu, H Y
- Wu, W J
- Yamamoto, J
- Yang, C H
- Dna binding protein
- Lyase
- Oxidoreductase
- Photoreduction
- Redox state