5mz6

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of a Separase-Securin complex from Caenorhabditis elegans at 3.8 A resolution

5mz6, resolution 3.80Å

Structural highlights

5mz6 is a 2 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.8Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SEP1_CAEEL Cysteine protease, which plays a central role in homologous chromosome separation during meiosis I and in sister chromatid separation during embryonic mitosis (PubMed:11728305, PubMed:12498686, PubMed:20116245, PubMed:21878498). Promotes chromosome/sister chromatid segregation by cleaving the scc-1 (mitosis) and rec-8 (meiosis) subunits of the cohesin complex at the onset of anaphase (Probable). May cleave histone H3-like protein cpar-1 during meiosis I metaphase-anaphase transition (PubMed:25919583). Promotes cortical granule exocytosis after oocyte fertilization during the first meiotic anaphase (PubMed:17913784, PubMed:21878498). Essential for embryonic cytokinesis by regulating rab-11-positive vesicle trafficking at the plasma membrane at the cleavage furrow and midbody (PubMed:20116245). Regulates centriole segregation during spermatocyte meiosis (PubMed:23401519). Required for embryonic anterior-posterior axis formation (PubMed:11832245).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8]

Publication Abstract from PubMed

Separase is a caspase-family protease that initiates chromatid segregation by cleaving the kleisin subunits (Scc1 and Rec8) of cohesin, and regulates centrosome duplication and mitotic spindle function through cleavage of kendrin and Slk19. To understand the mechanisms of securin regulation of separase, we used single-particle cryo-electron microscopy (cryo-EM) to determine a near-atomic-resolution structure of the Caenorhabditis elegans separase-securin complex. Separase adopts a triangular-shaped bilobal architecture comprising an N-terminal tetratricopeptide repeat (TPR)-like alpha-solenoid domain docked onto the conserved C-terminal protease domain. Securin engages separase in an extended antiparallel conformation, interacting with both lobes. It inhibits separase by interacting with the catalytic site through a pseudosubstrate mechanism, thus revealing that in the inhibited separase-securin complex, the catalytic site adopts a conformation compatible with substrate binding. Securin is protected from cleavage because an aliphatic side chain at the P1 position represses protease activity by disrupting the organization of catalytic site residues.

Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution.,Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D Nat Struct Mol Biol. 2017 Mar 6. doi: 10.1038/nsmb.3386. PMID:28263324^[9]

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

References

↑ Siomos MF, Badrinath A, Pasierbek P, Livingstone D, White J, Glotzer M, Nasmyth K. Separase is required for chromosome segregation during meiosis I in Caenorhabditis elegans. Curr Biol. 2001 Nov 27;11(23):1825-35. PMID:11728305 doi:10.1016/s0960-9822(01)00588-7
↑ Rappleye CA, Tagawa A, Lyczak R, Bowerman B, Aroian RV. The anaphase-promoting complex and separin are required for embryonic anterior-posterior axis formation. Dev Cell. 2002 Feb;2(2):195-206. PMID:11832245 doi:10.1016/s1534-5807(02)00114-4
↑ Kitagawa R, Law E, Tang L, Rose AM. The Cdc20 homolog, FZY-1, and its interacting protein, IFY-1, are required for proper chromosome segregation in Caenorhabditis elegans. Curr Biol. 2002 Dec 23;12(24):2118-23. PMID:12498686 doi:10.1016/s0960-9822(02)01392-1
↑ Bembenek JN, Richie CT, Squirrell JM, Campbell JM, Eliceiri KW, Poteryaev D, Spang A, Golden A, White JG. Cortical granule exocytosis in C. elegans is regulated by cell cycle components including separase. Development. 2007 Nov;134(21):3837-48. PMID:17913784 doi:10.1242/dev.011361
↑ Bembenek JN, White JG, Zheng Y. A role for separase in the regulation of RAB-11-positive vesicles at the cleavage furrow and midbody. Curr Biol. 2010 Feb 9;20(3):259-64. PMID:20116245 doi:10.1016/j.cub.2009.12.045
↑ Richie CT, Bembenek JN, Chestnut B, Furuta T, Schumacher JM, Wallenfang M, Golden A. Protein phosphatase 5 is a negative regulator of separase function during cortical granule exocytosis in C. elegans. J Cell Sci. 2011 Sep 1;124(Pt 17):2903-13. PMID:21878498 doi:10.1242/jcs.073379
↑ Schvarzstein M, Pattabiraman D, Bembenek JN, Villeneuve AM. Meiotic HORMA domain proteins prevent untimely centriole disengagement during Caenorhabditis elegans spermatocyte meiosis. Proc Natl Acad Sci U S A. 2013 Mar 5;110(10):E898-907. PMID:23401519 doi:10.1073/pnas.1213888110
↑ Monen J, Hattersley N, Muroyama A, Stevens D, Oegema K, Desai A. Separase Cleaves the N-Tail of the CENP-A Related Protein CPAR-1 at the Meiosis I Metaphase-Anaphase Transition in C. elegans. PLoS One. 2015 Apr 28;10(4):e0125382. PMID:25919583 doi:10.1371/journal.pone.0125382
↑ Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. Nat Struct Mol Biol. 2017 Mar 6. doi: 10.1038/nsmb.3386. PMID:28263324 doi:http://dx.doi.org/10.1038/nsmb.3386

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/5mz6"

@@ Line 3: / Line 3: @@
 <SX load='5mz6' size='340' side='right' viewer='molstar' caption='[[5mz6]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5mz6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MZ6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5mz6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MZ6 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sep-1, CELE_Y47G6A.12, Y47G6A.12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL]), ify-1, C27A2.3, CELE_C27A2.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</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=5mz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mz6 OCA], [http://pdbe.org/5mz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mz6 RCSB], [http://www.ebi.ac.uk/pdbsum/5mz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mz6 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=5mz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mz6 OCA], [https://pdbe.org/5mz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mz6 RCSB], [https://www.ebi.ac.uk/pdbsum/5mz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mz6 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SEP1_CAEEL SEP1_CAEEL] Cysteine protease, which plays a central role in homologous chromosome separation during meiosis I and in sister chromatid separation during embryonic mitosis (PubMed:11728305, PubMed:12498686, PubMed:20116245, PubMed:21878498). Promotes chromosome/sister chromatid segregation by cleaving the scc-1 (mitosis) and rec-8 (meiosis) subunits of the cohesin complex at the onset of anaphase (Probable). May cleave histone H3-like protein cpar-1 during meiosis I metaphase-anaphase transition (PubMed:25919583). Promotes cortical granule exocytosis after oocyte fertilization during the first meiotic anaphase (PubMed:17913784, PubMed:21878498). Essential for embryonic cytokinesis by regulating rab-11-positive vesicle trafficking at the plasma membrane at the cleavage furrow and midbody (PubMed:20116245). Regulates centriole segregation during spermatocyte meiosis (PubMed:23401519). Required for embryonic anterior-posterior axis formation (PubMed:11832245).<ref>PMID:11728305</ref> <ref>PMID:11832245</ref> <ref>PMID:12498686</ref> <ref>PMID:17913784</ref> <ref>PMID:20116245</ref> <ref>PMID:21878498</ref> <ref>PMID:23401519</ref> <ref>PMID:25919583</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </SX>
-[[Category: Caeel]]
+[[Category: Caenorhabditis elegans]]
 [[Category: Large Structures]]
-[[Category: Bai, X C]]
+[[Category: Bai XC]]
-[[Category: Barford, D]]
+[[Category: Barford D]]
-[[Category: Boland, A]]
+[[Category: Boland A]]
-[[Category: Chang, L]]
+[[Category: Chang L]]
-[[Category: Martin, T G]]
+[[Category: Martin TG]]
-[[Category: Scheres, S H.W]]
+[[Category: Scheres SHW]]
-[[Category: Yang, J]]
+[[Category: Yang J]]
-[[Category: Zhang, Z]]
+[[Category: Zhang Z]]
-[[Category: Caspase]]
-[[Category: Cell cycle]]
-[[Category: Cleavage]]
-[[Category: Cohesin]]

5mz6

From Proteopedia

Current revision

Cryo-EM structure of a Separase-Securin complex from Caenorhabditis elegans at 3.8 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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