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PDBsum entry 1ooj

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protein metals links
Metal binding protein PDB id
1ooj

 

 

 

 

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Contents
Protein chain
141 a.a. *
Metals
_CA ×4
Waters ×91
* Residue conservation analysis
PDB id:
1ooj
Name: Metal binding protein
Title: Structural genomics of caenorhabditis elegans : calmodulin
Structure: Calmodulin cmd-1. Chain: a. Engineered: yes
Source: Caenorhabditis elegans. Organism_taxid: 6239. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.11Å     R-factor:   0.212     R-free:   0.271
Authors: J.Symersky,G.Lin,S.Li,S.Qiu,C.-H.Luan,D.Luo,J.Tsao,M.Carson, L.Delucas,M.Luo,Southeast Collaboratory For Structural Genomics (Secsg)
Key ref:
J.Symersky et al. (2003). Structural genomics of caenorhabditis elegans: crystal structure of calmodulin. Proteins, 53, 947-949. PubMed id: 14635136 DOI: 10.1002/prot.10517
Date:
03-Mar-03     Release date:   25-Mar-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
O16305  (CALM_CAEEL) -  Calmodulin from Caenorhabditis elegans
Seq:
Struc:
149 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1002/prot.10517 Proteins 53:947-949 (2003)
PubMed id: 14635136  
 
 
Structural genomics of caenorhabditis elegans: crystal structure of calmodulin.
J.Symersky, G.Lin, S.Li, S.Qiu, M.Carson, N.Schormann, M.Luo.
 
  ABSTRACT  
 

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (Top) A stereo view of CaM superpositions based on C- positions of the N-terminal domains (residues 9-71). The C. elegans CaM (PDB code: 1OOJ) is shown as an orange ribbon with silver calcium spheres. The N- and C-termini are labeled. The other CaM's are shown in one color with smaller ribbons and spheres: 3CLN,[8] white; 4CLN,[9] lavender; 1CLL,[10] yellow; 1OSA,[12] green; 1EXR,[13] cyan. (Bottom) A close-up of the central helices with the same coloring and superposition as above. The helical centers were fitted to a circle to determine the radius of curvature (116 Å for C. elegans CaM). The circular arcs in cyan (1EXR, radius 63 Å) and yellow (1CLL, radius 72 Å) show the fits for the atomic-resolution fungal and human CaM, respectively.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2003, 53, 947-949) copyright 2003.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18175311 E.Laine, J.D.Yoneda, A.Blondel, and T.E.Malliavin (2008).
The conformational plasticity of calmodulin upon calcium complexation gives a model of its interaction with the oedema factor of Bacillus anthracis.
  Proteins, 71, 1813-1829.  
17552906 S.L.Russell, N.V.McFerran, E.M.Hoey, A.Trudgett, and D.J.Timson (2007).
Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica.
  Biol Chem, 388, 593-599.  
16721661 K.Chen, J.Ruan, and L.A.Kurgan (2006).
Prediction of three dimensional structure of calmodulin.
  Protein J, 25, 57-70.  
  18629163 , (2004).
Current awareness on comparative and functional genomics.
  Comp Funct Genomics, 5, 373-380.  
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.

 

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