1smh
From Proteopedia
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|PDB= 1smh |SIZE=350|CAPTION= <scene name='initialview01'>1smh</scene>, resolution 2.044Å | |PDB= 1smh |SIZE=350|CAPTION= <scene name='initialview01'>1smh</scene>, resolution 2.044Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene> | + | |LIGAND= <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=MG8:N-OCTANOYL-N-METHYLGLUCAMINE'>MG8</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span> |
|GENE= PRKACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= PRKACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1smh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1smh OCA], [http://www.ebi.ac.uk/pdbsum/1smh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1smh RCSB]</span> | ||
}} | }} | ||
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[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Kinzel, V.]] | [[Category: Kinzel, V.]] | ||
| - | [[Category: BU3]] | ||
| - | [[Category: MG8]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
| - | [[Category: | + | [[Category: camp-dependent protein kinase]] |
| + | [[Category: membrane]] | ||
| + | [[Category: myristoylation]] | ||
| + | [[Category: phosphorylation]] | ||
| + | [[Category: pka]] | ||
| + | [[Category: posttranslational modification]] | ||
| + | [[Category: protein kinase some]] | ||
| + | [[Category: ser10]] | ||
| + | [[Category: signaling]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:44:06 2008'' |
Revision as of 20:44, 30 March 2008
| |||||||
| , resolution 2.044Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | PRKACA (Bos taurus) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Protein kinase A variant complex with completely ordered N-terminal helix
Overview
Protein kinases comprise the major enzyme family critically involved in signal transduction pathways; posttranslational modifications affect their regulation and determine signaling states. The prototype protein kinase A (PKA) possesses an N-terminal alpha-helix (Helix A) that is atypical for kinases and is thus a major distinguishing feature of PKA. Its physiological function may involve myristoylation at the N-terminus and modulation via phosphorylation at serine 10. Here we describe an unusual structure of an unmyristoylated PKA, unphosphorylated at serine 10, with a completely ordered N-terminus. Using standard conditions (e.g., PKI 5-24, ATP site ligand, MEGA-8), a novel 2-fold phosphorylated PKA variant showed the ordered N-terminus in a new crystal packing arrangement. Thus, the critical factor for structuring the N-terminus is apparently the absence of phosphorylation of Ser10. The flexibility of the N-terminus, its myristoylation, and the conformational dependence on the phosphorylation state are consistent with a functional role for myristoylation.
About this Structure
1SMH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution., Breitenlechner C, Engh RA, Huber R, Kinzel V, Bossemeyer D, Gassel M, Biochemistry. 2004 Jun 22;43(24):7743-9. PMID:15196017
Page seeded by OCA on Sun Mar 30 23:44:06 2008
Categories: Bos taurus | Non-specific serine/threonine protein kinase | Protein complex | Bossemeyer, D. | Breitenlechner, C. | Engh, R A. | Gassel, M. | Huber, R. | Kinzel, V. | Alpha helix | Camp-dependent protein kinase | Membrane | Myristoylation | Phosphorylation | Pka | Posttranslational modification | Protein kinase some | Ser10 | Signaling
