8kfv
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of ZmMOC1 K229A in complex with a nicked Holliday junction soaked in Mn2+ for 180 seconds== | |
| + | <StructureSection load='8kfv' size='340' side='right'caption='[[8kfv]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8kfv]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8KFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KFV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=8kfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8kfv OCA], [https://pdbe.org/8kfv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8kfv RCSB], [https://www.ebi.ac.uk/pdbsum/8kfv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8kfv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B4FCI7_MAIZE B4FCI7_MAIZE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Holliday junction resolution is a crucial process in homologous recombination and DNA double-strand break repair. Complete Holliday junction resolution requires two stepwise incisions across the center of the junction, but the precise mechanism of metal ion-catalyzed Holliday junction cleavage remains elusive. Here, we perform a metal ion-triggered catalysis in crystals to investigate the mechanism of Holliday junction cleavage by MOC1. We capture the structures of MOC1 in complex with a nicked Holliday junction at various catalytic states, including the ground state, the one-metal ion binding state, and the two-metal ion binding state. Moreover, we also identify a third metal ion that may aid in the nucleophilic attack on the scissile phosphate. Further structural and biochemical analyses reveal a metal ion-mediated allosteric regulation between the two active sites, contributing to the enhancement of the second strand cleavage following the first strand cleavage, as well as the precise symmetric cleavage across the Holliday junction. Our work provides insights into the mechanism of metal ion-catalyzed Holliday junction resolution by MOC1, with implications for understanding how cells preserve genome integrity during the Holliday junction resolution phase. | ||
| - | + | MOC1 cleaves Holliday junctions through a cooperative nick and counter-nick mechanism mediated by metal ions.,Zhang D, Xu S, Luo Z, Lin Z Nat Commun. 2024 Jun 17;15(1):5140. doi: 10.1038/s41467-024-49490-9. PMID:38886375<ref>PMID:38886375</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8kfv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Zea mays]] | ||
| + | [[Category: Lin Z]] | ||
| + | [[Category: Luo Z]] | ||
| + | [[Category: Zhang D]] | ||
Current revision
Crystal structure of ZmMOC1 K229A in complex with a nicked Holliday junction soaked in Mn2+ for 180 seconds
| |||||||||||
Categories: Large Structures | Zea mays | Lin Z | Luo Z | Zhang D
