|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4xh0' size='340' side='right'caption='[[4xh0]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='4xh0' size='340' side='right'caption='[[4xh0]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xh0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_2001 Atcc 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XH0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xh0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata Candida glabrata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XH0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xhg|4xhg]], [[4xhh|4xhh]], [[4xhl|4xhl]]</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=4xh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh0 OCA], [https://pdbe.org/4xh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xh0 RCSB], [https://www.ebi.ac.uk/pdbsum/4xh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh0 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=4xh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xh0 OCA], [http://pdbe.org/4xh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4xh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xh0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6FS46_CANGA Q6FS46_CANGA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 2001]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Corbett KD]] |
| - | [[Category: Corbett, K D]] | + | [[Category: Ye Q]] |
| - | [[Category: Ye, Q]] | + | |
| - | [[Category: Casein kinase]]
| + | |
| - | [[Category: Monopolin]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q6FS46_CANGA
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
|
