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==Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP and phosphorylated peptide pSP20== | ==Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP and phosphorylated peptide pSP20== | ||
<StructureSection load='4ib1' size='340' side='right' caption='[[4ib1]], [[Resolution|resolution]] 1.63Å' scene=''> | <StructureSection load='4ib1' size='340' side='right'caption='[[4ib1]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ib1]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ib1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IB1 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4ib1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ib1 OCA], [https://pdbe.org/4ib1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ib1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ib1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ib1 ProSAT]</span></td></tr> | |||
</table> | |||
<tr | |||
<table> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
X-ray structures of several ternary | X-ray structures of several ternary product complexes of the catalytic subunit of cAMP-dependent protein kinase (PKAc) have been determined with no bound metal ions and with Na(+) or K(+) coordinated at two metal-binding sites. The metal-free PKAc and the enzyme with alkali metals were able to facilitate the phosphoryl transfer reaction. In all studied complexes, the ATP and the substrate peptide (SP20) were modified into the products ADP and the phosphorylated peptide. The products of the phosphotransfer reaction were also found when ATP-gammaS, a nonhydrolyzable ATP analogue, reacted with SP20 in the PKAc active site containing no metals. Single turnover enzyme kinetics measurements utilizing (32)P-labeled ATP confirmed the phosphotransferase activity of the enzyme in the absence of metal ions and in the presence of alkali metals. In addition, the structure of the apo-PKAc binary complex with SP20 suggests that the sequence of binding events may become ordered in a metal-free environment, with SP20 binding first to prime the enzyme for subsequent ATP binding. Comparison of these structures reveals conformational and hydrogen bonding changes that might be important for the mechanism of catalysis. | ||
Metal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl Transfer.,Gerlits O, Das A, Keshwani MM, Taylor S, Waltman MJ, Langan P, Heller WT, Kovalevsky A Biochemistry. 2014 May 20;53(19):3179-86. doi: 10.1021/bi5000965. Epub 2014 May, 8. PMID:24786636<ref>PMID:24786636</ref> | |||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ib1" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CAMP-dependent protein kinase 3D structures|CAMP-dependent protein kinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Gerlits O]] | ||
[[Category: | [[Category: Kovalevsky A]] | ||
Latest revision as of 06:02, 21 November 2024
Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP and phosphorylated peptide pSP20Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP and phosphorylated peptide pSP20
Structural highlights
Publication Abstract from PubMedX-ray structures of several ternary product complexes of the catalytic subunit of cAMP-dependent protein kinase (PKAc) have been determined with no bound metal ions and with Na(+) or K(+) coordinated at two metal-binding sites. The metal-free PKAc and the enzyme with alkali metals were able to facilitate the phosphoryl transfer reaction. In all studied complexes, the ATP and the substrate peptide (SP20) were modified into the products ADP and the phosphorylated peptide. The products of the phosphotransfer reaction were also found when ATP-gammaS, a nonhydrolyzable ATP analogue, reacted with SP20 in the PKAc active site containing no metals. Single turnover enzyme kinetics measurements utilizing (32)P-labeled ATP confirmed the phosphotransferase activity of the enzyme in the absence of metal ions and in the presence of alkali metals. In addition, the structure of the apo-PKAc binary complex with SP20 suggests that the sequence of binding events may become ordered in a metal-free environment, with SP20 binding first to prime the enzyme for subsequent ATP binding. Comparison of these structures reveals conformational and hydrogen bonding changes that might be important for the mechanism of catalysis. Metal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl Transfer.,Gerlits O, Das A, Keshwani MM, Taylor S, Waltman MJ, Langan P, Heller WT, Kovalevsky A Biochemistry. 2014 May 20;53(19):3179-86. doi: 10.1021/bi5000965. Epub 2014 May, 8. PMID:24786636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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