1smh: Difference between revisions
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[[Image:1smh.gif|left|200px]] | [[Image:1smh.gif|left|200px]] | ||
'''Protein kinase A variant complex with completely ordered N-terminal helix''' | {{Structure | ||
|PDB= 1smh |SIZE=350|CAPTION= <scene name='initialview01'>1smh</scene>, resolution 2.044Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene> and <scene name='pdbligand=MG8:N-OCTANOYL-N-METHYLGLUCAMINE'>MG8</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] | |||
|GENE= PRKACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |||
}} | |||
'''Protein kinase A variant complex with completely ordered N-terminal helix''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SMH is a [ | 1SMH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15196017 15196017] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
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[[Category: pka; protein kinase a; camp-dependent protein kinase; phosphorylation; ser10; myristoylation; posttranslational modification; signaling; membrane]] | [[Category: pka; protein kinase a; camp-dependent protein kinase; phosphorylation; ser10; myristoylation; posttranslational modification; signaling; membrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:52 2008'' | ||
Revision as of 15:06, 20 March 2008
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| , resolution 2.044Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | PRKACA (Bos taurus) | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Protein kinase A variant complex with completely ordered N-terminal helix
OverviewOverview
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 StructureAbout this Structure
1SMH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 14:06:52 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Bos taurus
- Non-specific serine/threonine protein kinase
- Protein complex
- Bossemeyer, D.
- Breitenlechner, C.
- Engh, R A.
- Gassel, M.
- Huber, R.
- Kinzel, V.
- BU3
- MG8
- Alpha helix
- Pka; protein kinase a; camp-dependent protein kinase; phosphorylation; ser10; myristoylation; posttranslational modification; signaling; membrane