1CTP

STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND AN INHIBITOR PEPTIDE DISPLAYS AN OPEN CONFORMATION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Observed: 0.190 

wwPDB Validation 3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation.

Karlsson, R.Zheng, J.Xuong, N.Taylor, S.S.Sowadski, J.M.

(1993) Acta Crystallogr D Biol Crystallogr 49: 381-388

  • DOI: 10.1107/S0907444993002306
  • Structures With Same Primary Citation

  • PubMed Abstract: 
  • The crystal structure of a binary complex of the porcine heart catalytic (C) subunit of cAMP-dependent protein kinase (space group P4(1)32; a = 171.5 A) complexed with a di-iodinated peptide inhibitor, PKI(5-24), has been solved and refined to 2.9 A ...

    The crystal structure of a binary complex of the porcine heart catalytic (C) subunit of cAMP-dependent protein kinase (space group P4(1)32; a = 171.5 A) complexed with a di-iodinated peptide inhibitor, PKI(5-24), has been solved and refined to 2.9 A resolution with an overall R of 21.1%. The r.m.s. deviations from ideal bond lengths and angles are 0.022 A and 4.3 degrees. A single isotropic B of 17 A(2) was used for all atoms. The structure solution was carried out initially by molecular replacement of electron density followed by refinement against atomic coordinates from orthorhombic crystals of a binary complex of the mouse recombinant enzyme previously described [Knighton, Zheng, Ten Eyck, Ashford, Xuong, Taylor & Sowadski (1991). Science, 253, 407-414]. The most striking difference between the two crystal structures is a large displacement of the small lobe of the enzyme. In the cubic crystal, the beta-sheet of the small lobe is rotated by 15 degrees and translated by 1.9 A with respect to the orthorhombic crystal. Possible explanations for why this binary complex crystallized in an open conformation in contrast to a similar binary complex of the recombinant enzyme are discussed. This study demonstrates that considerable information about parts of a crystal structure can be obtained without a complete crystal structure analysis. Specifically, the six rigid-group parameters of a poly alanine model of the beta-structure were obtained satisfactorily from a crystal structure by refinement of difference Fourier coefficients based on an approximate partial structure model.


    Related Citations: 
    • Crystal-Structure of the Catalytic Subunit of Camp-Dependent Protein-Kinase Complexed with a Mgatp and Peptide Inhibitor
      Zheng, J., Knighton, D.R., Xuong, N.-H., Eyck, L.F.T., Karlsson, R., Taylor, S.S., Sowadski, J.M.
      (1993) Biochemistry 32: 2154
    • 2.0 Angstroms Refined Crystal Structure of the Catalytic Subunit of Camp-Dependent Protein Kinase Complexed with a Peptide Inhibitor and Detergent
      Knighton, D.R., Bell, S.M., Zheng, J., Eyck, L.F.T., Xuong, N.-H., Taylor, S.S., Sowadski, J.M.
      (1993) Acta Crystallogr D Biol Crystallogr 49: 357
    • 2.2 Angstroms Refined Crystal-Structure of the Catalytic Subunit of Camp-Dependent Protein-Kinase Complexed with Mnatp and a Peptide Inhibitor
      Zheng, J.H., Trafny, E.A., Knighton, D.R., Xuong, N.-H., Taylor, S.S., Eyck, L.F.T., Sowadski, J.M.
      (1993) Acta Crystallogr D Biol Crystallogr 49: 362
    • Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
      Knighton, D.R., Zheng, J., Eyck, L.F.T., Ashford, V.A., Xuong, N.-H., Taylor, S.S., Sowadski, J.M.
      (1991) Science 253: 407
    • Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase
      Knighton, D.R., Zheng, J., Eyck, L.F.T., Xuong, N.-H., Taylor, S.S., Sowadski, J.M.
      (1991) Science 253: 414
    • Expression of the Catalytic Subunit of Camp-Dependent Protein Kinase in Escherichia Coli
      Slice, L.W., Taylor, S.S.
      (1989) J Biol Chem 264: 20940

    Organizational Affiliation

    Department of Medicine, University of California, San Diego, La Jolla 92093-0654, USA.



Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
cAMP-DEPENDENT PROTEIN KINASE
E
350Sus scrofaMutation(s): 0 
Gene Names: PRKACA
EC: 2.7.1.37 (PDB Primary Data), 2.7.11.11 (UniProt)
Find proteins for P36887 (Sus scrofa)
Go to UniProtKB:  P36887
Protein Feature View
  • Reference Sequence
  • Find similar proteins by: Sequence   |   Structure
Entity ID: 2
MoleculeChainsSequence LengthOrganismDetails
cAMP-dependent protein kinase inhibitor, alpha form
I
20Homo sapiensMutation(s): 0 
Find proteins for P61926 (Oryctolagus cuniculus)
Go to UniProtKB:  P61926
Protein Feature View
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
MYR
Query on MYR

Download CCD File 
E
MYRISTIC ACID
C14 H28 O2
TUNFSRHWOTWDNC-UHFFFAOYSA-N
 Ligand Interaction
Modified Residues  2 Unique
IDChainsTypeFormula2D DiagramParent
TPO
Query on TPO
EL-PEPTIDE LINKINGC4 H10 N O6 PTHR
TYI
Query on TYI
IL-PEPTIDE LINKINGC9 H9 I2 N O3TYR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Observed: 0.190 
  • Space Group: P 41 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 171.5α = 90
b = 171.5β = 90
c = 171.5γ = 90
Software Package:
Software NamePurpose
TNTrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 1994-01-31
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2012-07-18
    Changes: Source and taxonomy