3dls
From Proteopedia
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==Crystal structure of human PAS kinase bound to ADP== | ==Crystal structure of human PAS kinase bound to ADP== | ||
| - | <StructureSection load='3dls' size='340' side='right' caption='[[3dls]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3dls' size='340' side='right'caption='[[3dls]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3dls]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3dls]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DLS FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id=' | + | <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=MG:MAGNESIUM+ION'>MG</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=3dls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dls OCA], [https://pdbe.org/3dls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dls RCSB], [https://www.ebi.ac.uk/pdbsum/3dls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dls ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/3dls TOPSAN]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PASK_HUMAN PASK_HUMAN] Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation.<ref>PMID:16275910</ref> <ref>PMID:17052199</ref> <ref>PMID:17595531</ref> <ref>PMID:21181396</ref> <ref>PMID:21418524</ref> <ref>PMID:20943661</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dls ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3dls ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Per-Arnt-Sim (PAS) domain-containing protein kinase (PASK) is an evolutionary conserved protein kinase that coordinates cellular metabolism with metabolic demand in yeast and mammals. The molecular mechanisms underlying PASK regulation, however, remain unknown. Herein, we describe a crystal structure of the kinase domain of human PASK, which provides insights into the regulatory mechanisms governing catalysis. We show that the kinase domain adopts an active conformation and has catalytic activity in vivo and in vitro in the absence of activation loop phosphorylation. Using site-directed mutagenesis and structural comparison with active and inactive kinases, we identified several key structural features in PASK that enable activation loop phosphorylation-independent activity. Finally, we used combinatorial peptide library screening to determine that PASK prefers basic residues at the P-3 and P-5 positions in substrate peptides. Our results describe the key features of the PASK structure and how those features are important for PASK activity and substrate selection. | ||
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| - | Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation.,Kikani CK, Antonysamy SA, Bonanno JB, Romero R, Zhang FF, Russell M, Gheyi T, Iizuka M, Emtage S, Sauder JM, Turk BE, Burley SK, Rutter J J Biol Chem. 2010 Dec 24;285(52):41034-43. Epub 2010 Oct 13. PMID:20943661<ref>PMID:20943661</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3dls" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Antonysamy | + | [[Category: Antonysamy S]] |
| - | [[Category: Bonanno | + | [[Category: Bonanno JB]] |
| - | [[Category: Burley | + | [[Category: Burley SK]] |
| - | [[Category: Gheyi | + | [[Category: Gheyi T]] |
| - | [[Category: Iizuka | + | [[Category: Iizuka M]] |
| - | + | [[Category: Romero R]] | |
| - | [[Category: Romero | + | [[Category: Russell M]] |
| - | [[Category: Russell | + | [[Category: Rutter J]] |
| - | [[Category: Rutter | + | [[Category: Sauder JM]] |
| - | [[Category: Sauder | + | [[Category: Wasserman SR]] |
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Current revision
Crystal structure of human PAS kinase bound to ADP
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Categories: Homo sapiens | Large Structures | Antonysamy S | Bonanno JB | Burley SK | Gheyi T | Iizuka M | Romero R | Russell M | Rutter J | Sauder JM | Wasserman SR
