4xhg
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4xhg is ON HOLD until Paper Publication Authors: Ye, Q., Corbett, K.D. Description: Structure of C. glabrata Hrr25 bound to ADP (formate condition)...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of C. glabrata Hrr25 bound to ADP (formate condition)== | |
| + | <StructureSection load='4xhg' size='340' side='right'caption='[[4xhg]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4xhg]] 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=4XHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XHG FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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=FMT:FORMIC+ACID'>FMT</scene></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=4xhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xhg OCA], [https://pdbe.org/4xhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xhg RCSB], [https://www.ebi.ac.uk/pdbsum/4xhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xhg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6FS46_CANGA Q6FS46_CANGA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:27491543</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Corbett | + | <div class="pdbe-citations 4xhg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ye | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Corbett KD]] | ||
| + | [[Category: Ye Q]] | ||
Current revision
Structure of C. glabrata Hrr25 bound to ADP (formate condition)
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