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| | ==Structure of S. cerevisiae Hrr25 1-394 (K38R mutant)== | | ==Structure of S. cerevisiae Hrr25 1-394 (K38R mutant)== |
| - | <StructureSection load='4xhl' size='340' side='right' caption='[[4xhl]], [[Resolution|resolution]] 3.01Å' scene=''> | + | <StructureSection load='4xhl' size='340' side='right'caption='[[4xhl]], [[Resolution|resolution]] 3.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xhl]] is a 1 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=4XHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XHL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xhl]] is a 1 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=4XHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XHL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CKI:N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE'>CKI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.01Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xh0|4xh0]], [[4xhg|4xhg]], [[4xhh|4xhh]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CKI:N-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE'>CKI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HRR25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=4xhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xhl OCA], [https://pdbe.org/4xhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xhl RCSB], [https://www.ebi.ac.uk/pdbsum/4xhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xhl ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4xhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xhl OCA], [http://pdbe.org/4xhl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xhl RCSB], [http://www.ebi.ac.uk/pdbsum/4xhl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xhl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HRR25_YEAST HRR25_YEAST]] Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate. | + | [https://www.uniprot.org/uniprot/HRR25_YEAST HRR25_YEAST] Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate. |
| | <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: Non-specific serine/threonine protein kinase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Corbett KD]] |
| - | [[Category: Ye, Q]] | + | [[Category: Ye Q]] |
| - | [[Category: Casein kinase]]
| + | |
| - | [[Category: Monopolin]]
| + | |
| - | [[Category: Transferase-transferase inhibitor complex]]
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| Structural highlights
Function
HRR25_YEAST Associated with repair of damaged DNA and meiosis. Phosphorylates serine and threonine. Can use casein as a substrate.
Publication Abstract from PubMed
In budding yeast, the monopolin complex mediates sister kinetochore cross-linking and co-orientation in meiosis I. The CK1delta kinase Hrr25 is critical for sister kinetochore co-orientation, but its roles are not well understood. Here, we present the structures of Hrr25 and its complex with the monopolin subunit Mam1. Hrr25 possesses a "central domain" that packs tightly against the kinase C-lobe, adjacent to the binding site for Mam1. Together, the Hrr25 central domain and Mam1 form a novel, contiguous embellishment to the Hrr25 kinase domain that affects Hrr25 conformational dynamics and enzyme kinetics. Mam1 binds a hydrophobic surface on the Hrr25 N-lobe that is conserved in CK1delta-family kinases, suggesting a role for this surface in recruitment and/or regulation of these enzymes throughout eukaryotes. Finally, using purified proteins, we find that Hrr25 phosphorylates the kinetochore receptor for monopolin, Dsn1. Together with our new structural insights into the fully assembled monopolin complex, this finding suggests that tightly localized Hrr25 activity modulates monopolin complex-kinetochore interactions through phosphorylation of both kinetochore and monopolin complex components.
Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator.,Ye Q, Ur SN, Su TY, Corbett KD EMBO J. 2016 Oct 4;35(19):2139-2151. Epub 2016 Aug 4. PMID:27491543[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ye Q, Ur SN, Su TY, Corbett KD. Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator. EMBO J. 2016 Oct 4;35(19):2139-2151. Epub 2016 Aug 4. PMID:27491543 doi:http://dx.doi.org/10.15252/embj.201694082
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