6mf6
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6mf6' size='340' side='right'caption='[[6mf6]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='6mf6' size='340' side='right'caption='[[6mf6]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6mf6]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MF6 OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6mf6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MF6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MF6 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC5, MSD2, PKX2, YMR001C, YM8270.03C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), DBF4, DNA52, YDR052C, D4205, YD9609.07C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </span></td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6mf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mf6 OCA], [http://pdbe.org/6mf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mf6 RCSB], [http://www.ebi.ac.uk/pdbsum/6mf6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mf6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CDC5_YEAST CDC5_YEAST]] Protein kinase required for the cell cycle where it is involved in mitotic exit. A component of the fear (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Phosphorylates SCC1/MCD1 and NET1.<ref>PMID:11371343</ref> <ref>PMID:11832211</ref> <ref>PMID:12056824</ref> [[http://www.uniprot.org/uniprot/DBF4_YEAST DBF4_YEAST]] Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.<ref>PMID:8066465</ref> <ref>PMID:12441400</ref> <ref>PMID:16319063</ref> <ref>PMID:17018296</ref> <ref>PMID:19013276</ref> <ref>PMID:18245450</ref> <ref>PMID:19692334</ref> <ref>PMID:19478884</ref> <ref>PMID:20436286</ref> <ref>PMID:21036905</ref> <ref>PMID:20170732</ref> <ref>PMID:20054399</ref> | [[http://www.uniprot.org/uniprot/CDC5_YEAST CDC5_YEAST]] Protein kinase required for the cell cycle where it is involved in mitotic exit. A component of the fear (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Phosphorylates SCC1/MCD1 and NET1.<ref>PMID:11371343</ref> <ref>PMID:11832211</ref> <ref>PMID:12056824</ref> [[http://www.uniprot.org/uniprot/DBF4_YEAST DBF4_YEAST]] Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.<ref>PMID:8066465</ref> <ref>PMID:12441400</ref> <ref>PMID:16319063</ref> <ref>PMID:17018296</ref> <ref>PMID:19013276</ref> <ref>PMID:18245450</ref> <ref>PMID:19692334</ref> <ref>PMID:19478884</ref> <ref>PMID:20436286</ref> <ref>PMID:21036905</ref> <ref>PMID:20170732</ref> <ref>PMID:20054399</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polo-like kinases (Plks) are key cell cycle regulators. They contain a kinase domain followed by a polo-box domain that recognizes phosphorylated substrates and enhances their phosphorylation. The regulatory subunit of the Dbf4-dependent kinase complex interacts with the polo-box domain of Cdc5 (the sole Plk in Saccharomyces cerevisiae) in a phosphorylation-independent manner. We have solved the crystal structures of the polo-box domain of Cdc5 on its own and in the presence of peptides derived from Dbf4 and a canonical phosphorylated substrate. The structure bound to the Dbf4-peptide reveals an additional density on the surface opposite to the phospho-peptide binding site that allowed us to propose a model for the interaction. We found that the two peptides can bind simultaneously and non-competitively to the polo-box domain in solution. Furthermore, point mutations on the surface opposite to the phosphopeptide binding site of the polo-box domain disrupt the interaction with the Dbf4 peptide in solution and cause an early anaphase arrest phenotype distinct from the mitotic exit defect typically observed in cdc5 mutants. Collectively, our data illustrates the importance of non-canonical interactions mediated by the polo-box domain and provide key mechanistic insights into the combinatorial recognition of substrates by Polo-like kinases. | ||
| + | |||
| + | Distinct surfaces on Cdc5/PLK Polo-box domain orchestrate combinatorial substrate recognition during cell division.,Almawi AW, Langlois-Lemay L, Boulton S, Rodriguez Gonzalez J, Melacini G, D'Amours D, Guarne A Sci Rep. 2020 Feb 25;10(1):3379. doi: 10.1038/s41598-020-60344-4. PMID:32099015<ref>PMID:32099015</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6mf6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Baker's yeast]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Polo kinase]] | [[Category: Polo kinase]] | ||
Revision as of 07:02, 2 September 2020
Crystal structure of budding yeast Cdc5 polo-box domain in complex with the Dbf4 polo-interacting region.
| |||||||||||
