1smh
From Proteopedia
(New page: 200px<br /><applet load="1smh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1smh, resolution 2.044Å" /> '''Protein kinase A va...) |
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| - | [[Image:1smh.gif|left|200px]]<br /><applet load="1smh" size=" | + | [[Image:1smh.gif|left|200px]]<br /><applet load="1smh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1smh, resolution 2.044Å" /> | caption="1smh, resolution 2.044Å" /> | ||
'''Protein kinase A variant complex with completely ordered N-terminal helix'''<br /> | '''Protein kinase A variant complex with completely ordered N-terminal helix'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein kinases comprise the major enzyme family critically involved in | + | 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== | ==About this Structure== | ||
| - | 1SMH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with BU3 and MG8 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1SMH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=BU3:'>BU3</scene> and <scene name='pdbligand=MG8:'>MG8</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bossemeyer, D.]] | [[Category: Bossemeyer, D.]] | ||
[[Category: Breitenlechner, C.]] | [[Category: Breitenlechner, C.]] | ||
| - | [[Category: Engh, R | + | [[Category: Engh, R A.]] |
[[Category: Gassel, M.]] | [[Category: Gassel, M.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
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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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:04 2008'' |
Revision as of 13:03, 21 February 2008
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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 with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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 Thu Feb 21 15:03:04 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. | BU3 | MG8 | Alpha helix | Pka; protein kinase a; camp-dependent protein kinase; phosphorylation; ser10; myristoylation; posttranslational modification; signaling; membrane
