PDBsum entry 2jww

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Metal binding protein PDB id
Protein chain
109 a.a. *
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Calcium-free rat alpha-parvalbumin
Structure: Parvalbumin alpha. Chain: a. Engineered: yes
Source: Rattus norvegicus. Rat. Gene: pvalb, pva. Expressed in: escherichia coli.
NMR struc: 20 models
Authors: M.T.Henzl,J.J.Tanner
Key ref:
M.T.Henzl and J.J.Tanner (2008). Solution structure of Ca2+-free rat alpha-parvalbumin. Protein Sci, 17, 431-438. PubMed id: 18218708 DOI: 10.1110/ps.073318308
25-Oct-07     Release date:   12-Aug-08    
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Protein chain
Pfam   ArchSchema ?
P02625  (PRVA_RAT) -  Parvalbumin alpha
110 a.a.
109 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   7 terms 
  Biological process     cytosolic calcium ion homeostasis   1 term 
  Biochemical function     protein homodimerization activity     4 terms  


DOI no: 10.1110/ps.073318308 Protein Sci 17:431-438 (2008)
PubMed id: 18218708  
Solution structure of Ca2+-free rat alpha-parvalbumin.
M.T.Henzl, J.J.Tanner.
Mammals express two parvalbumins-an alpha isoform and a beta isoform. In rat, the alpha-parvalbumin (alpha-PV) exhibits superior divalent ion affinity. For example, the standard free energies for Ca2+ binding differ by 5.5 kcal/mol in 0.15 M KCl (pH 7.4). High-resolution structures of the Ca2+-bound proteins provide little insight into this disparity, prompting a structural analysis of the apo-proteins. A recent analysis of rat beta-PV suggested that Ca2+ removal provokes substantial conformational changes-reorientation of the C, D, and E helices; reorganization of the hydrophobic core; reduced interdomain contact; and remodeling of the AB domain. The energetic penalty attendant to reversing these changes, it was suggested, could contribute to the attenuated divalent ion-binding signature of that protein. That hypothesis is supported by data presented herein, describing the solution structure and peptide backbone dynamics of Ca2+-free rat alpha-PV. In marked contrast to rat beta-PV, the apo- and Ca2+-loaded forms of the rat alpha isoform are quite similar. Significant structural differences appear to be confined to the loop regions of the molecule. This finding implies that the alpha-PV isoform enjoys elevated divalent ion affinity because the metal ion-binding events do not require major structural rearrangement and the concomitant sacrifice of binding energy.
  Selected figure(s)  
Figure 2.
Figure 2. Solution structure of Ca^2+-free rat -PV. An ensemble of the 20 lowest energy structures determined with ARIA-CNS. This figure and Figures 3, 5, and 6 were produced with PyMOL (DeLano Scientific).
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2008, 17, 431-438) copyright 2008.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21287610 M.T.Henzl, J.J.Tanner, and A.Tan (2011).
Solution structures of chicken parvalbumin 3 in the Ca(2+) -free and Ca(2+) -bound states.
  Proteins, 79, 752-764.
PDB codes: 2kyc 2kyf
20156445 J.P.Schuermann, A.Tan, J.J.Tanner, and M.T.Henzl (2010).
Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states.
  J Mol Biol, 397, 991.
PDB codes: 2kqy 3fs7
19387850 B.A.Tikunov, and L.C.Rome (2009).
Is high concentration of parvalbumin a requirement for superfast relaxation?
  J Muscle Res Cell Motil, 30, 57-65.  
19622856 F.Hoh, A.Cavé, M.P.Strub, J.L.Banères, and A.Padilla (2009).
Removing the invariant salt bridge of parvalbumin increases flexibility in the AB-loop structure.
  Acta Crystallogr D Biol Crystallogr, 65, 733-743.
PDB code: 3f45
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