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3ost

From Proteopedia

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Current revision (10:36, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3ost' size='340' side='right'caption='[[3ost]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
<StructureSection load='3ost' size='340' side='right'caption='[[3ost]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ost]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OST FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ost]] 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=3OST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OST FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.694&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3osm|3osm]], [[3ose|3ose]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCC4, YCL024W, YCL24W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=3ost FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ost OCA], [https://pdbe.org/3ost PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ost RCSB], [https://www.ebi.ac.uk/pdbsum/3ost PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ost ProSAT]</span></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=3ost FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ost OCA], [https://pdbe.org/3ost PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ost RCSB], [https://www.ebi.ac.uk/pdbsum/3ost PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ost ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KCC4_YEAST KCC4_YEAST]] Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis.<ref>PMID:12773812</ref>
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[https://www.uniprot.org/uniprot/KCC4_YEAST KCC4_YEAST] Involved in regulation of bud growth during cell cycle and in septin organization. Plays a role in cell wall synthesis.<ref>PMID:12773812</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phospholipid-binding modules such as PH, C1, and C2 domains play crucial roles in location-dependent regulation of many protein kinases. Here, we identify the KA1 domain (kinase associated-1 domain), found at the C terminus of yeast septin-associated kinases (Kcc4p, Gin4p, and Hsl1p) and human MARK/PAR1 kinases, as a membrane association domain that binds acidic phospholipids. Membrane localization of isolated KA1 domains depends on phosphatidylserine. Using X-ray crystallography, we identified a structurally conserved binding site for anionic phospholipids in KA1 domains from Kcc4p and MARK1. Mutating this site impairs membrane association of both KA1 domains and intact proteins and reveals the importance of phosphatidylserine for bud neck localization of yeast Kcc4p. Our data suggest that KA1 domains contribute to "coincidence detection," allowing kinases to bind other regulators (such as septins) only at the membrane surface. These findings have important implications for understanding MARK/PAR1 kinases, which are implicated in Alzheimer's disease, cancer, and autism.
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Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids.,Moravcevic K, Mendrola JM, Schmitz KR, Wang YH, Slochower D, Janmey PA, Lemmon MA Cell. 2010 Dec 10;143(6):966-77. PMID:21145462<ref>PMID:21145462</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ost" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Lemmon, M A]]
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[[Category: Lemmon MA]]
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[[Category: Moravcevic, K]]
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[[Category: Moravcevic K]]
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[[Category: Kinase]]
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[[Category: Lipid binding protein]]
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[[Category: Membrane association]]
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[[Category: Transferase]]
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Current revision

Structure of the Kinase Associated-1 (KA1) from Kcc4p

PDB ID 3ost

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