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6bzg

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Revision as of 06:58, 27 March 2019

Structure of S. cerevisiae Zip2:Spo16 complex, P212121 form

Structural highlights

6bzg is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	6bzf
Gene:	ZIP2 (ATCC 18824), SPO16 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] [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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ San-Segundo PA, Roeder GS. Pch2 links chromatin silencing to meiotic checkpoint control. Cell. 1999 Apr 30;97(3):313-24. PMID:10319812
↑ Bailis JM, Smith AV, Roeder GS. Bypass of a meiotic checkpoint by overproduction of meiotic chromosomal proteins. Mol Cell Biol. 2000 Jul;20(13):4838-48. PMID:10848609
↑ Agarwal S, Roeder GS. Zip3 provides a link between recombination enzymes and synaptonemal complex proteins. Cell. 2000 Jul 21;102(2):245-55. PMID:10943844
↑ Novak JE, Ross-Macdonald PB, Roeder GS. The budding yeast Msh4 protein functions in chromosome synapsis and the regulation of crossover distribution. Genetics. 2001 Jul;158(3):1013-25. PMID:11454751
↑ Peoples-Holst TL, Burgess SM. Multiple branches of the meiotic recombination pathway contribute independently to homolog pairing and stable juxtaposition during meiosis in budding yeast. Genes Dev. 2005 Apr 1;19(7):863-74. doi: 10.1101/gad.1293605. PMID:15805472 doi:http://dx.doi.org/10.1101/gad.1293605
↑ Tsubouchi T, Zhao H, Roeder GS. The meiosis-specific zip4 protein regulates crossover distribution by promoting synaptonemal complex formation together with zip2. Dev Cell. 2006 Jun;10(6):809-19. doi: 10.1016/j.devcel.2006.04.003. PMID:16740482 doi:http://dx.doi.org/10.1016/j.devcel.2006.04.003
↑ Chua PR, Roeder GS. Zip2, a meiosis-specific protein required for the initiation of chromosome synapsis. Cell. 1998 May 1;93(3):349-59. PMID:9590170
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6bzg"

@@ Line 1: / Line 1: @@
 ==Structure of S. cerevisiae Zip2:Spo16 complex, P212121 form==
-<StructureSection load='6bzg' size='340' side='right' caption='[[6bzg]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
+<StructureSection load='6bzg' size='340' side='right'caption='[[6bzg]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6bzg]] is a 2 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=6BZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZG FirstGlance]. <br>
@@ Line 25: / Line 25: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Arora, K]]
 [[Category: Corbett, K D]]

6bzg

From Proteopedia

Revision as of 06:58, 27 March 2019

Structure of S. cerevisiae Zip2:Spo16 complex, P212121 form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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