PDBsum entry 2kne

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protein metals Protein-protein interface(s) links
Metal transport PDB id
Protein chains
148 a.a. *
28 a.a. *
_CA ×4
* Residue conservation analysis
PDB id:
Name: Metal transport
Title: Calmodulin wraps around its binding domain in the plasma membrane ca2+ pump anchored by a novel 18-1 motif
Structure: Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Atpase, ca++ transporting, plasma membrane 4. Chain: b. Fragment: unp residues 1086-1113, c28. Engineered: yes. Other_details: calmodulin binding domain of pmca c-tail
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21(de3)-plyss. Gene: calm, calm1, calm2, calm3, calml2, cam, cam1, cam2, cam3, camb, camc, camiii. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3.
NMR struc: 20 models
Authors: N.Juranic,E.Atanasova,A.G.Filoteo,S.Macura,F.G.Prendergast, J.T.Penniston,E.E.Strehler
Key ref: N.Juranic et al. (2010). Calmodulin wraps around its binding domain in the plasma membrane Ca2+ pump anchored by a novel 18-1 motif. J Biol Chem, 285, 4015-4024. PubMed id: 19996092
21-Aug-09     Release date:   24-Nov-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P62158  (CALM_HUMAN) -  Calmodulin
149 a.a.
148 a.a.
Protein chain
Pfam   ArchSchema ?
P23634  (AT2B4_HUMAN) -  Plasma membrane calcium-transporting ATPase 4
1241 a.a.
28 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.  - Calcium-transporting ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2)
+ H(2)O
+ Ca(2+)(Side 1)
+ phosphate
+ Ca(2+)(Side 2)
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   17 terms 
  Biological process     Fc-epsilon receptor signaling pathway   54 terms 
  Biochemical function     enzyme regulator activity     21 terms  


J Biol Chem 285:4015-4024 (2010)
PubMed id: 19996092  
Calmodulin wraps around its binding domain in the plasma membrane Ca2+ pump anchored by a novel 18-1 motif.
N.Juranic, E.Atanasova, A.G.Filoteo, S.Macura, F.G.Prendergast, J.T.Penniston, E.E.Strehler.
Using solution NMR spectroscopy, we obtained the structure of Ca(2+)-calmodulin (holoCaM) in complex with peptide C28 from the binding domain of the plasma membrane Ca(2+)-ATPase (PMCA) pump isoform 4b. This provides the first atomic resolution insight into the binding mode of holoCaM to the full-length binding domain of PMCA. Structural comparison of the previously determined holoCaM.C20 complex with this holoCaM.C28 complex supports the idea that the initial binding step is represented by (holoCaM.C20) and the final bound complex by (holoCaM.C28). This affirms the existing multi-step kinetic model of PMCA4b activation by CaM. The complex exhibits a new binding motif in which holoCaM is wrapped around helical C28 peptide using two anchoring residues from the peptide at relative positions 18 and 1. The anchors correspond to Phe-1110 and Trp-1093, respectively, in full-length PMCA4b, and the peptide and CaM are oriented in an anti-parallel manner. This is a greater sequence distance between anchors than in any of the known holoCaM complexes with a helical peptide. Analysis of the geometry of holoCaM-peptide binding for the cases where the target peptide adopts an alpha(D)-helix with its anchors buried in the main hydrophobic pockets of the two CaM lobes establishes that only relative sequential positions of 10, 14, 17, and 18 are allowed for the second anchor.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23086147 H.Tidow, L.R.Poulsen, A.Andreeva, M.Knudsen, K.L.Hein, C.Wiuf, M.G.Palmgren, and P.Nissen (2012).
A bimodular mechanism of calcium control in eukaryotes.
  Nature, 491, 468-472.
PDB code: 4aqr
20653564 H.Tokumitsu, N.Hatano, M.Tsuchiya, S.Yurimoto, T.Fujimoto, N.Ohara, R.Kobayashi, and H.Sakagami (2010).
Identification and characterization of PRG-1 as a neuronal calmodulin-binding protein.
  Biochem J, 431, 81-91.  
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