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5fby

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Revision as of 06:45, 19 July 2023

Crystal structure of ctSPD

Structural highlights

5fby is a 2 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.898Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G0SHM3_CHATD

Publication Abstract from PubMed

Accurate chromosome segregation requires timely dissolution of chromosome cohesion after chromosomes are properly attached to the mitotic spindle. Separase is absolutely essential for cohesion dissolution in organisms from yeast to man. It cleaves the kleisin subunit of cohesin and opens the cohesin ring to allow chromosome segregation. Cohesin cleavage is spatiotemporally controlled by separase-associated regulatory proteins, including the inhibitory chaperone securin, and by phosphorylation of both the enzyme and substrates. Dysregulation of this process causes chromosome missegregation and aneuploidy, contributing to cancer and birth defects. Despite its essential functions, atomic structures of separase have not been determined. Here we report crystal structures of the separase protease domain from the thermophilic fungus Chaetomium thermophilum, alone or covalently bound to unphosphorylated and phosphorylated inhibitory peptides derived from a cohesin cleavage site. These structures reveal how separase recognizes cohesin and how cohesin phosphorylation by polo-like kinase 1 (Plk1) enhances cleavage. Consistent with a previous cellular study, mutating two securin residues in a conserved motif that partly matches the separase cleavage consensus converts securin from a separase inhibitor to a substrate. Our study establishes atomic mechanisms of substrate cleavage by separase and suggests competitive inhibition by securin.

Structural basis of cohesin cleavage by separase.,Lin Z, Luo X, Yu H Nature. 2016 Apr 7;532(7597):131-4. doi: 10.1038/nature17402. Epub 2016 Mar 30. PMID:27027290^[1]

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

References

↑ Lin Z, Luo X, Yu H. Structural basis of cohesin cleavage by separase. Nature. 2016 Apr 7;532(7597):131-4. doi: 10.1038/nature17402. Epub 2016 Mar 30. PMID:27027290 doi:http://dx.doi.org/10.1038/nature17402

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/5fby"

@@ Line 1: / Line 1: @@
 ==Crystal structure of ctSPD==
-<StructureSection load='5fby' size='340' side='right' caption='[[5fby]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5fby' size='340' side='right'caption='[[5fby]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5fby]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FBY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5fby]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FBY FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fc2|5fc2]], [[5fc3|5fc3]]</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]] 1.898&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0070540 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=5fby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fby OCA], [https://pdbe.org/5fby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fby RCSB], [https://www.ebi.ac.uk/pdbsum/5fby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fby ProSAT]</span></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=5fby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fby OCA], [http://pdbe.org/5fby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fby RCSB], [http://www.ebi.ac.uk/pdbsum/5fby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fby ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/G0SHM3_CHATD G0SHM3_CHATD]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Chatd]]
+[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
-[[Category: Synthetic construct sequences]]
+[[Category: Large Structures]]
-[[Category: Lin, Z]]
+[[Category: Synthetic construct]]
-[[Category: Luo, X]]
+[[Category: Lin Z]]
-[[Category: Yu, H]]
+[[Category: Luo X]]
-[[Category: Cohesin]]
+[[Category: Yu H]]
-[[Category: Complex]]
-[[Category: Hydrolase]]

5fby

From Proteopedia

Revision as of 06:45, 19 July 2023

Crystal structure of ctSPD

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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