PDBsum entry 1smh

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protein ligands Protein-protein interface(s) links
Signaling protein,transferase/inhibitor PDB id
Protein chains
350 a.a. *
20 a.a. *
BU3 ×6
Waters ×175
* Residue conservation analysis
PDB id:
Name: Signaling protein,transferase/inhibitor
Title: Protein kinase a variant complex with completely ordered n- terminal helix
Structure: Camp-dependent protein kinase, alpha-catalytic subunit. Chain: a. Fragment: catalytic subunit. Synonym: pka c-alpha. Engineered: yes. Mutation: yes. Camp-dependent protein kinase inhibitor, alpha form.
Source: Bos taurus. Cattle. Organism_taxid: 9913. Gene: prkaca. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: peptide synthesis. This sequence occurs naturally in humans
Biol. unit: Dimer (from PQS)
2.04Å     R-factor:   0.191     R-free:   0.238
Authors: C.Breitenlechner,R.A.Engh,R.Huber,V.Kinzel,D.Bossemeyer, M.Gassel
Key ref:
C.Breitenlechner et al. (2004). The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution. Biochemistry, 43, 7743-7749. PubMed id: 15196017 DOI: 10.1021/bi0362525
09-Mar-04     Release date:   06-Jul-04    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P00517  (KAPCA_BOVIN) -  cAMP-dependent protein kinase catalytic subunit alpha
351 a.a.
350 a.a.*
Protein chain
Pfam   ArchSchema ?
P61926  (IPKA_RABIT) -  cAMP-dependent protein kinase inhibitor alpha
76 a.a.
20 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.  - cAMP-dependent protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     sperm midpiece   11 terms 
  Biological process     regulation of proteasomal protein catabolic process   18 terms 
  Biochemical function     nucleotide binding     13 terms  


DOI no: 10.1021/bi0362525 Biochemistry 43:7743-7749 (2004)
PubMed id: 15196017  
The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution.
C.Breitenlechner, R.A.Engh, R.Huber, V.Kinzel, D.Bossemeyer, M.Gassel.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
17407165 K.S.Sandhu, and D.Dash (2007).
Dynamic alpha-helices: conformations that do not conform.
  Proteins, 68, 109-122.  
16895917 S.S.Yeong, Y.Zhu, D.Smith, C.Verma, W.G.Lim, B.J.Tan, Q.T.Li, N.S.Cheung, M.Cai, Y.Z.Zhu, S.F.Zhou, S.L.Tan, and W.Duan (2006).
The last 10 amino acid residues beyond the hydrophobic motif are critical for the catalytic competence and function of protein kinase Calpha.
  J Biol Chem, 281, 30768-30781.  
16505477 Y.Liu, N.V.Belkina, C.Graham, and S.Shaw (2006).
Independence of protein kinase C-delta activity from activation loop phosphorylation: structural basis and altered functions in cells.
  J Biol Chem, 281, 12102-12111.  
16253959 J.Wu, J.Yang, N.Kannan, Madhusudan, N.H.Xuong, L.F.Ten Eyck, and S.S.Taylor (2005).
Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix.
  Protein Sci, 14, 2871-2879.
PDB code: 1syk
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