5xyn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of Csm2-Psy3-Shu1-Shu2 complex from budding yeast== |
| + | <StructureSection load='5xyn' size='340' side='right' caption='[[5xyn]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xyn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XYN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xyn OCA], [http://pdbe.org/5xyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xyn RCSB], [http://www.ebi.ac.uk/pdbsum/5xyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xyn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SHU2_YEAST SHU2_YEAST]] Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase. Required for error-free repair of spontaneous and induced DNA lesions to protect the genome from mutation.<ref>PMID:12972632</ref> <ref>PMID:15654096</ref> <ref>PMID:17671161</ref> <ref>PMID:19496932</ref> [[http://www.uniprot.org/uniprot/PSY3_YEAST PSY3_YEAST]] Required for resistance to the DNA-damaging agents methyl methanesulfonate (MMS), cisplatin and oxaliplatin, but not to mitomycin C. Plays a role in protection against mutation accumulation. May be a component of the recombination-repair pathway.<ref>PMID:12149442</ref> <ref>PMID:12482937</ref> <ref>PMID:12972632</ref> <ref>PMID:15173006</ref> <ref>PMID:15654096</ref> <ref>PMID:19496932</ref> [[http://www.uniprot.org/uniprot/SHU1_YEAST SHU1_YEAST]] Plays a role in a RAD51/RAD54-dependent homologous recombination repair (HRR) pathway to repair MMS-induced lesions during S-phase.<ref>PMID:15654096</ref> <ref>PMID:19496932</ref> [[http://www.uniprot.org/uniprot/CSM2_YEAST CSM2_YEAST]] Involved in chromosome segregation during meiosis. Promotes efficient recombinational repair and functions in the protection of the genome from spontaneous and induced DNA damage like mutations and gross chromosomal rearrangements (GCRs).<ref>PMID:11470404</ref> <ref>PMID:12972632</ref> <ref>PMID:15184655</ref> <ref>PMID:15654096</ref> <ref>PMID:19496932</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Shu complex, a conserved regulator consisting of Csm2, Psy3, Shu1 and Shu2 in budding yeast, plays an important role in the assembly of the Rad51-ssDNA filament in homologous recombination. However, the molecular basis for the assembly of the Shu complex and its functional role in DNA repair is still elusive. Here, we report the crystal structure of the yeast Shu complex, revealing that Csm2, Psy3, Shu1 and Shu2 interact with each other in sequence to form a V-shape overall structure. Shu1 adopts a structure resembling the ATPase core domain of Rad51 and represents a new Rad51 paralog. Shu2 assumes a novel structural fold consisting of a conserved zinc-finger containing SWIM domain and a small insertion domain. The functional roles of the key residues are validated using mutagenesis and in vitro pull-down and in vivo yeast growth studies. Structural analysis together with available biological data identifies two potential DNA-binding sites, one of which might be responsible for binding the ssDNA region of the 3'-overhang DNA and the other for the dsDNA region. Collectively, these findings reveal the molecular basis for the assembly of the Shu complex and shed new insight on its functional role in homologous recombination. | ||
| - | + | Structural basis for the functional role of the Shu complex in homologous recombination.,Zhang S, Wang L, Tao Y, Bai T, Lu R, Zhang T, Chen J, Ding J Nucleic Acids Res. 2017 Oct 24. doi: 10.1093/nar/gkx992. PMID:29069504<ref>PMID:29069504</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5xyn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ding, J]] | ||
| + | [[Category: Zhang, S]] | ||
| + | [[Category: Zhang, T]] | ||
| + | [[Category: Comlex]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Replication]] | ||
Revision as of 07:38, 8 November 2017
The crystal structure of Csm2-Psy3-Shu1-Shu2 complex from budding yeast
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