5xw4

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Current revision (08:16, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5xw4' size='340' side='right'caption='[[5xw4]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='5xw4' size='340' side='right'caption='[[5xw4]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xw4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XW4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XW4 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw4 OCA], [http://pdbe.org/5xw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw4 OCA], [https://pdbe.org/5xw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xw4 RCSB], [https://www.ebi.ac.uk/pdbsum/5xw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CDC14_YEAST CDC14_YEAST]] Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphosprylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus.<ref>PMID:11511359</ref> <ref>PMID:12737806</ref> <ref>PMID:14993267</ref> <ref>PMID:15004526</ref> <ref>PMID:15137939</ref> <ref>PMID:15190202</ref> <ref>PMID:15917648</ref> <ref>PMID:17116692</ref> <ref>PMID:18235228</ref> <ref>PMID:18287090</ref> <ref>PMID:18595708</ref> <ref>PMID:19158678</ref> <ref>PMID:19339280</ref> <ref>PMID:20619650</ref> <ref>PMID:20660629</ref> <ref>PMID:20923974</ref> <ref>PMID:20980394</ref> <ref>PMID:21127052</ref> <ref>PMID:21690308</ref> <ref>PMID:21784165</ref> <ref>PMID:22072794</ref> <ref>PMID:22078879</ref> <ref>PMID:22117071</ref> <ref>PMID:22363215</ref> <ref>PMID:22454527</ref> <ref>PMID:22872148</ref> <ref>PMID:7021319</ref> <ref>PMID:8668128</ref> <ref>PMID:9295359</ref> <ref>PMID:9885559</ref>
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[https://www.uniprot.org/uniprot/CDC14_YEAST CDC14_YEAST] Protein phosphatase which antagonizes mitotic cyclin-dependent kinase CDC28, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases. Allows damaged actomyosin rings to be maintained to facilitate completion of cell division in response to minor perturbation of the cell division machinery. Inhibits transcription of ribosomal genes (rDNA) during anaphase and controls segregation of nucleolus by facilitating condensin targeting to rDNA chromatin in anaphase. Dephosphorylates SIC1, a CDC28 inhibitor, and SWI5, a transcription factor for SIC1, and induces degradation of mitotic cyclins, likely by dephosphorylating the activator of mitotic cyclin degradation, CDH1. Dephosphorylates the microtubule bundling factor ASE1 which is required to define a centered and focused mitotic spindle midzone that can drive continuous spindle elongation. Dephosphorylates the anaphase-promoting complex inhibitor ACM1, leading to its degradation. Facilitates INN1-CYK3 complex formation which promotes cytokinesis through the dephosphosprylation of CDC28-phosphosphorylated INN1. Reverts also the inhibitory CDC28 phosphorylation of CHS2 for endoplasmic reticulum export, ensuring that septum formation is contingent upon chromosome separation and exit from mitosis. Additional substrates for CDC14 are the formins BNI1 and BNR1, as well as CDC6, DBP2, DSN1, INCENP, KAR9, MCM3, ORC2, ORC6, SLD2, and SWI6. Activity is inhibited by interaction with NET1 which sequesters it to the nucleolus.<ref>PMID:11511359</ref> <ref>PMID:12737806</ref> <ref>PMID:14993267</ref> <ref>PMID:15004526</ref> <ref>PMID:15137939</ref> <ref>PMID:15190202</ref> <ref>PMID:15917648</ref> <ref>PMID:17116692</ref> <ref>PMID:18235228</ref> <ref>PMID:18287090</ref> <ref>PMID:18595708</ref> <ref>PMID:19158678</ref> <ref>PMID:19339280</ref> <ref>PMID:20619650</ref> <ref>PMID:20660629</ref> <ref>PMID:20923974</ref> <ref>PMID:20980394</ref> <ref>PMID:21127052</ref> <ref>PMID:21690308</ref> <ref>PMID:21784165</ref> <ref>PMID:22072794</ref> <ref>PMID:22078879</ref> <ref>PMID:22117071</ref> <ref>PMID:22363215</ref> <ref>PMID:22454527</ref> <ref>PMID:22872148</ref> <ref>PMID:7021319</ref> <ref>PMID:8668128</ref> <ref>PMID:9295359</ref> <ref>PMID:9885559</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Kobayashi, J]]
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[[Category: Kobayashi J]]
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[[Category: Matsuura, Y]]
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[[Category: Matsuura Y]]
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[[Category: Cell cycle]]
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[[Category: Phosphatase]]
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Current revision

Crystal structure of budding yeast Cdc14p (wild type) in the apo state

PDB ID 5xw4

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