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[[ | ==Crystal structure of R194A mutant of cAMP-dependent protein kinase with unphosphorylated activation loop== | ||
<StructureSection load='4dfy' size='340' side='right' caption='[[4dfy]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4dfy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DFY FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1atp|1atp]], [[1j3h|1j3h]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prkaca, Pkaca ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/cAMP-dependent_protein_kinase cAMP-dependent protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.11 2.7.11.11] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dfy RCSB], [http://www.ebi.ac.uk/pdbsum/4dfy PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The catalytic subunit of cAMP-dependent protein kinase (PKA) is a member of the AGC subfamily of protein kinases. While PKA has served as a structural model for the protein kinase superfamily, all previous structures of the catalytic subunit contain a phosphorylated activation loop. To understand the structural effects of activation loop phosphorylation at Thr197 we used a PKA mutant which does not autophosphorylate at Thr197. The enzyme crystallized in the apo-state and the structure was solved to 3.0 angstroms. The N-lobe is rotated by 18 degrees relative to the wild type apoenzyme which illustrates that the enzyme likely exists in a wide range of conformations in solution due to the uncoupling of the N- and C-lobes. Several regions of the protein including the activation loop are disordered in the structure and there are alternate main chain conformations for the magnesium positioning loop and catalytic loop causing a complete loss of hydrogen bonding between these two active site structural elements. These alterations are reflected in a 20-fold decrease in the apparent phosphoryl transfer rate as measured by pre-steady-state kinetic methods. | |||
Structural basis for the regulation of protein kinase A by activation loop phosphorylation.,Steichen JM, Kuchinskas M, Keshwani MM, Yang J, Adams JA, Taylor SS J Biol Chem. 2012 Feb 10. PMID:22334660<ref>PMID:22334660</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[CAMP-dependent protein kinase|CAMP-dependent protein kinase]] | |||
*[[Eukaryotic Protein Kinase Catalytic Domain|Eukaryotic Protein Kinase Catalytic Domain]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: CAMP-dependent protein kinase]] | [[Category: CAMP-dependent protein kinase]] | ||
Revision as of 10:15, 5 June 2014
Crystal structure of R194A mutant of cAMP-dependent protein kinase with unphosphorylated activation loopCrystal structure of R194A mutant of cAMP-dependent protein kinase with unphosphorylated activation loop
Structural highlights
Publication Abstract from PubMedThe catalytic subunit of cAMP-dependent protein kinase (PKA) is a member of the AGC subfamily of protein kinases. While PKA has served as a structural model for the protein kinase superfamily, all previous structures of the catalytic subunit contain a phosphorylated activation loop. To understand the structural effects of activation loop phosphorylation at Thr197 we used a PKA mutant which does not autophosphorylate at Thr197. The enzyme crystallized in the apo-state and the structure was solved to 3.0 angstroms. The N-lobe is rotated by 18 degrees relative to the wild type apoenzyme which illustrates that the enzyme likely exists in a wide range of conformations in solution due to the uncoupling of the N- and C-lobes. Several regions of the protein including the activation loop are disordered in the structure and there are alternate main chain conformations for the magnesium positioning loop and catalytic loop causing a complete loss of hydrogen bonding between these two active site structural elements. These alterations are reflected in a 20-fold decrease in the apparent phosphoryl transfer rate as measured by pre-steady-state kinetic methods. Structural basis for the regulation of protein kinase A by activation loop phosphorylation.,Steichen JM, Kuchinskas M, Keshwani MM, Yang J, Adams JA, Taylor SS J Biol Chem. 2012 Feb 10. PMID:22334660[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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