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| | ==Structure of S. cerevisiae Zip2:Spo16 complex, C2 form== | | ==Structure of S. cerevisiae Zip2:Spo16 complex, C2 form== |
| - | <StructureSection load='6bzf' size='340' side='right' caption='[[6bzf]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='6bzf' size='340' side='right'caption='[[6bzf]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bzf]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bzf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BZF FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M0H:S-(HYDROXYMETHYL)-L-CYSTEINE'>M0H</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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]] 2.286Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPO16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), ZIP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M0H:S-(HYDROXYMETHYL)-L-CYSTEINE'>M0H</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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=6bzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzf OCA], [http://pdbe.org/6bzf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bzf RCSB], [http://www.ebi.ac.uk/pdbsum/6bzf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzf ProSAT]</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=6bzf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzf OCA], [https://pdbe.org/6bzf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bzf RCSB], [https://www.ebi.ac.uk/pdbsum/6bzf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ZIP2_YEAST ZIP2_YEAST]] Required for initiation of meiotic chromosome synapsis. Involved in synaptonemal complex formation, a structure that tethers a pair of homologous chromosomes along their lengths and plays a central role in recombination and homolog segregation during meiosis. Required for the normal localization of MSH4 to chromosomes.<ref>PMID:10319812</ref> <ref>PMID:10848609</ref> <ref>PMID:10943844</ref> <ref>PMID:11454751</ref> <ref>PMID:15805472</ref> <ref>PMID:16740482</ref> <ref>PMID:9590170</ref> [[http://www.uniprot.org/uniprot/SPO16_YEAST SPO16_YEAST]] Necessary for efficient spore formation. | + | [https://www.uniprot.org/uniprot/SPO16_YEAST SPO16_YEAST] Necessary for efficient spore formation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Arora, K]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Arora K]] |
| - | [[Category: Dna binding protein]] | + | [[Category: Corbett KD]] |
| - | [[Category: Xpf-ercc1 meiosis recombination]]
| + | |
| Structural highlights
Function
SPO16_YEAST Necessary for efficient spore formation.
Publication Abstract from PubMed
In eukaryotic meiosis, generation of haploid gametes depends on the formation of inter-homolog crossovers, which enable the pairing, physical linkage, and eventual segregation of homologs in the meiosis I division. A class of conserved meiosis-specific proteins, collectively termed ZMMs, are required for formation and spatial control of crossovers throughout eukaryotes. Here, we show that three Saccharomyces cerevisiae ZMM proteins-Zip2, Zip4 and Spo16-interact with one another and form a DNA-binding complex critical for crossover formation and control. We determined the crystal structure of a Zip2:Spo16 subcomplex, revealing a heterodimer structurally related to the XPF:ERCC1 endonuclease complex. Zip2:Spo16 lacks an endonuclease active site, but binds specific DNA structures found in early meiotic recombination intermediates. Mutations in multiple DNA-binding surfaces on Zip2:Spo16 severely compromise DNA binding, supporting a model in which the complex's central and HhH domains cooperate to bind DNA. Overall, our data support a model in which the Zip2:Zip4:Spo16 complex binds and stabilizes early meiotic recombination intermediates, then coordinates additional factors to promote crossover formation and license downstream events including synaptonemal complex assembly.
The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding.,Arora K, Corbett KD Nucleic Acids Res. 2018 Dec 19. pii: 5253063. doi: 10.1093/nar/gky1273. PMID:30566683[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arora K, Corbett KD. The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding. Nucleic Acids Res. 2018 Dec 19. pii: 5253063. doi: 10.1093/nar/gky1273. PMID:30566683 doi:http://dx.doi.org/10.1093/nar/gky1273
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