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PDBsum entry 1atp
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Transferase(phosphotransferase) PDB id
1atp

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
336 a.a. *
20 a.a. *
Ligands
ATP
Metals
_MN ×2
Waters ×103
* Residue conservation analysis
PDB id:
1atp
Name: Transferase(phosphotransferase)
Title: 2.2 angstrom refined crystal structure of the catalytic subunit of camp-dependent protein kinase complexed with mnatp and a peptide inhibitor
Structure: Camp-dependent protein kinase. Chain: e. Engineered: yes. Peptide inhibitor pki(5-24). Chain: i. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090
Biol. unit: Dimer (from PQS)
Resolution:
2.20Å     R-factor:   0.177    
Authors: J.Zheng,E.A.Trafny,D.R.Knighton,N.-H.Xuong,S.S.Taylor,L.F.Teneyck, J.M.Sowadski
Key ref:
J.Zheng et al. (1993). 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr D Biol Crystallogr, 49, 362-365. PubMed id: 15299527 DOI: 10.1107/S0907444993000423
Date:
08-Jan-93     Release date:   15-Apr-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P05132  (KAPCA_MOUSE) -  cAMP-dependent protein kinase catalytic subunit alpha from Mus musculus
Seq:
Struc: 		351 a.a.
336 a.a.*
Protein chain
P63248  (IPKA_MOUSE) -  cAMP-dependent protein kinase inhibitor alpha from Mus musculus
Seq:
Struc: 		76 a.a.
20 a.a.
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain E: E.C.2.7.11.11  - cAMP-dependent protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
Bound ligand (Het Group name = ATP)
corresponds exactly 		+ ATP
 = O-phospho-L-seryl-[protein]
 + ADP
 + H(+)
L-threonyl-[protein]
Bound ligand (Het Group name = ATP)
corresponds exactly 		+ ATP
 = O-phospho-L-threonyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S0907444993000423 Acta Crystallogr D Biol Crystallogr 49:362-365 (1993)
PubMed id: 15299527  
 
 
2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor.
J.Zheng, E.A.Trafny, D.R.Knighton, N.H.Xuong, S.S.Taylor, L.F.Ten Eyck, J.M.Sowadski.
 
  ABSTRACT  
 
. The crystal structure of a ternary complex containing the catalytic subunit of cAMP-dependent protein kinase, ATP and a 20-residue inhibitor peptide was refined at a resolution of 2.2 A to an R value of 0.177. In order to identify the metal binding sites, the crystals, originally grown in the presence of low concentrations of Mg(2+), were soaked in Mn(2+). Two Mn(2+) ions were identified using an anomalous Fourier map. One Mn(2+) ion bridges the gamma- and beta-phosphates and interacts with Asp184 and two water molecules. The second Mn(2+) ion interacts with the side chains of Asn171 and Asp l84 as well as with a water molecule. Modeling a serine into the P site of the inhibitor peptide suggests a mechanism for phosphotransfer.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Environment of conserved amino acis surrounding the site of phosphotransfer. For this diagram a serine (shown in red) was modeled into the P site so that distances between the "y-phosphate and a protein substrate could be estimated. The primary metal site, OM382, is coordinated by the invariant Asp184, as well as two water molecules as indicated above. The secondary inhibitory metal site, OM383, is coordiated by the invariant Asnl7, by invariant Asp184, as well as by one water molecule. Asp14, therefore, is shared by both metal sites in this inhibited complex.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 362-365) copyright 1993.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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Large-scale shape changes in proteins and macromolecular complexes.
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Conformational diversity of catalytic cores of protein kinases.
  Pharmacol Ther, 82, 157-164.  
  10631989 M.C.Hutter, and V.Helms (1999).
Influence of key residues on the reaction mechanism of the cAMP-dependent protein kinase.
  Protein Sci, 8, 2728-2733.  
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The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation.
  Structure, 7, 1057-1065.
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10450084 S.Hayward (1999).
Structural principles governing domain motions in proteins.
  Proteins, 36, 425-435.  
10360180 T.Schindler, F.Sicheri, A.Pico, A.Gazit, A.Levitzki, and J.Kuriyan (1999).
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  Mol Cell, 3, 639-648.
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9857185 M.E.Cunningham, and L.A.Greene (1998).
A function-structure model for NGF-activated TRK.
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Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A.
  Proc Natl Acad Sci U S A, 95, 484-491.  
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Crystal structure of JNK3: a kinase implicated in neuronal apoptosis.
  Structure, 6, 983-991.
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9434895 F.Sicheri, and J.Kuriyan (1997).
Structures of Src-family tyrosine kinases.
  Curr Opin Struct Biol, 7, 777-785.  
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A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility.
  Structure, 5, 921-935.
PDB code: 1bkx
9312016 S.R.Hubbard (1997).
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog.
  EMBO J, 16, 5572-5581.
PDB code: 1ir3
8805593 C.D.Mol, J.M.Harris, E.M.McIntosh, and J.A.Tainer (1996).
Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits.
  Structure, 4, 1077-1092.
PDB codes: 1q5h 1q5u
8601311 J.Goldberg, A.C.Nairn, and J.Kuriyan (1996).
Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I.
  Cell, 84, 875-887.
PDB code: 1a06
9383464 K.Koide, M.E.Bunnage, L.Gomez Paloma, J.R.Kanter, S.S.Taylor, L.L.Brunton, and K.C.Nicolaou (1995).
Molecular design and biological activity of potent and selective protein kinase inhibitors related to balanol.
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7479711 U.Schulze-Gahmen, J.Brandsen, H.D.Jones, D.O.Morgan, L.Meijer, J.Vesely, and S.H.Kim (1995).
Multiple modes of ligand recognition: crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine.
  Proteins, 22, 378-391.
PDB codes: 1w0x 2exm
8048162 D.Bossemeyer (1994).
The glycine-rich sequence of protein kinases: a multifunctional element.
  Trends Biochem Sci, 19, 201-205.  
7517688 D.O.Morgan, and H.L.De Bondt (1994).
Protein kinase regulation: insights from crystal structure analysis.
  Curr Opin Cell Biol, 6, 239-246.  
8168546 J.P.Huggins, A.J.Ganzhorn, V.Saudek, J.T.Pelton, and R.A.Atkinson (1994).
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
  Eur J Biochem, 221, 581-593.  
7809124 M.Vihinen, D.Vetrie, H.S.Maniar, H.D.Ochs, Q.Zhu, I.Vorechovský, A.D.Webster, L.D.Notarangelo, L.Nilsson, and J.M.Sowadski (1994).
Structural basis for chromosome X-linked agammaglobulinemia: a tyrosine kinase disease.
  Proc Natl Acad Sci U S A, 91, 12803-12807.  
  8003955 Madhusudan, E.A.Trafny, N.H.Xuong, J.A.Adams, L.F.Ten Eyck, S.S.Taylor, and J.M.Sowadski (1994).
cAMP-dependent protein kinase: crystallographic insights into substrate recognition and phosphotransfer.
  Protein Sci, 3, 176-187.
PDB codes: 1jbp 1jlu
7712293 S.Cox, E.Radzio-Andzelm, and S.S.Taylor (1994).
Domain movements in protein kinases.
  Curr Opin Struct Biol, 4, 893-901.  
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Three protein kinase structures define a common motif.
  Structure, 2, 345-355.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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