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PDBsum entry 2f2p
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protein metals Protein-protein interface(s) links
Metal binding protein PDB id
2f2p

 

 

 

 

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Contents
Protein chains
169 a.a. *
Metals
_CA ×8
Waters ×29
* Residue conservation analysis
PDB id:
2f2p
Name: Metal binding protein
Title: Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode
Structure: Calmodulin fused with calmodulin-binding domain of calcineurin. Chain: a, b. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.234     R-free:   0.297
Authors: Q.Ye,A.Wong,Z.Jia
Key ref:
Q.Ye et al. (2006). Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode. Biochemistry, 45, 738-745. PubMed id: 16411749 DOI: 10.1021/bi0521801
Date:
17-Nov-05     Release date:   21-Feb-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P48452  (PP2BA_BOVIN) -  Protein phosphatase 3 catalytic subunit alpha from Bos taurus
Seq:
Struc: 		 
Seq:
Struc: 		521 a.a.
169 a.a.*
Protein chains
Pfam   ArchSchema ?
P62157  (CALM_BOVIN) -  Calmodulin from Bos taurus
Seq:
Struc: 		149 a.a.
169 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 137 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.16  - protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
O-phospho-L-seryl-[protein]
 + H2O
 = L-seryl-[protein]
 + phosphate
O-phospho-L-threonyl-[protein]
 + H2O
 = L-threonyl-[protein]
 + phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1021/bi0521801 Biochemistry 45:738-745 (2006)
PubMed id: 16411749  
 
 
Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode.
Q.Ye, X.Li, A.Wong, Q.Wei, Z.Jia.
 
  ABSTRACT  
 
Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21287611 S.E.O'Donnell, L.Yu, C.A.Fowler, and M.A.Shea (2011).
Recognition of β-calcineurin by the domains of calmodulin: Thermodynamic and structural evidence for distinct roles.
  Proteins, 79, 765-786.  
19827097 A.Rezvanpour, J.M.Phillips, and G.S.Shaw (2009).
Design of high-affinity S100-target hybrid proteins.
  Protein Sci, 18, 2528-2536.  
19667066 H.Ishida, M.Rainaldi, and H.J.Vogel (2009).
Structural studies of soybean calmodulin isoform 4 bound to the calmodulin-binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode.
  J Biol Chem, 284, 28292-28305.
PDB code: 2kn2
19404396 V.Majava, and P.Kursula (2009).
Domain swapping and different oligomeric States for the complex between calmodulin and the calmodulin-binding domain of calcineurin a.
  PLoS ONE, 4, e5402.
PDB code: 2w73
18488168 B.Wang, P.Zhang, and Q.Wei (2008).
Recent progress on the structure of Ser/Thr protein phosphatases.
  Sci China C Life Sci, 51, 487-494.  
18669651 M.I.Stefan, S.J.Edelstein, and N.Le Novère (2008).
An allosteric model of calmodulin explains differential activation of PP2B and CaMKII.
  Proc Natl Acad Sci U S A, 105, 10768-10773.  
18384083 Q.Ye, H.Wang, J.Zheng, Q.Wei, and Z.Jia (2008).
The complex structure of calmodulin bound to a calcineurin peptide.
  Proteins, 73, 19-27.
PDB code: 2r28
18819009 S.J.Abraham, S.Hoheisel, and V.Gaponenko (2008).
Detection of protein-ligand interactions by NMR using reductive methylation of lysine residues.
  J Biomol NMR, 42, 143-148.  
18461636 Y.Zhang, H.Tan, Z.Jia, and G.Chen (2008).
Ligand-induced dimer formation of calmodulin.
  J Mol Recognit, 21, 267-274.  
  17602618 A.M.Levin, K.Murase, P.J.Jackson, M.L.Flinspach, T.L.Poulos, and G.A.Weiss (2007).
Double barrel shotgun scanning of the caveolin-1 scaffolding domain.
  ACS Chem Biol, 2, 493-500.  
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 code is shown on the right.

 

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