1smh
From Proteopedia
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[[Image:1smh.gif|left|200px]] | [[Image:1smh.gif|left|200px]] | ||
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'''Protein kinase A variant complex with completely ordered N-terminal helix''' | '''Protein kinase A variant complex with completely ordered N-terminal helix''' | ||
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[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Kinzel, V.]] | [[Category: Kinzel, V.]] | ||
- | [[Category: | + | [[Category: Alpha helix]] |
- | [[Category: | + | [[Category: Camp-dependent protein kinase]] |
- | [[Category: | + | [[Category: Membrane]] |
- | [[Category: | + | [[Category: Myristoylation]] |
- | [[Category: | + | [[Category: Phosphorylation]] |
- | [[Category: | + | [[Category: Pka]] |
- | [[Category: | + | [[Category: Posttranslational modification]] |
- | [[Category: | + | [[Category: Protein kinase some]] |
- | [[Category: | + | [[Category: Ser10]] |
- | [[Category: | + | [[Category: Signaling]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:53:13 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 05:53, 3 May 2008
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 Sat May 3 08:53:13 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