PDBsum entry 2kax

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Metal binding protein PDB id
Protein chain
92 a.a. *
* Residue conservation analysis
PDB id:
Name: Metal binding protein
Title: Solution structure and dynamics of s100a5 in the apo and ca2+ -bound states
Structure: Protein s100-a5. Chain: a, b. Synonym: s100 calcium-binding protein a5, protein s-100d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 31 models
Authors: I.Bertini,S.Das Gupta,X.Hu,T.Karavelas,C.Luchinat,G.Parigi, J.Yuan,Structural Proteomics In Europe (Spine)
Key ref: I.Bertini et al. (2009). Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states. J Biol Inorg Chem, 14, 1097-1107. PubMed id: 19536568
17-Nov-08     Release date:   30-Jun-09    
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Protein chains
Pfam   ArchSchema ?
P33763  (S10A5_HUMAN) -  Protein S100-A5
92 a.a.
92 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     neuronal cell body   2 terms 
  Biochemical function     protein homodimerization activity     5 terms  


J Biol Inorg Chem 14:1097-1107 (2009)
PubMed id: 19536568  
Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states.
I.Bertini, S.Das Gupta, X.Hu, T.Karavelas, C.Luchinat, G.Parigi, J.Yuan.
S100A5 is a calcium binding protein of the S100 family, with one canonical and one S100-specific EF-hand motif per subunit. Although its function is still unknown, it has recently been reported to be one of the S100 proteins able to interact with the receptor for advanced glycation end products. The homodimeric solution structures of S100A5 in both the apo and the calcium(II)-loaded forms have been obtained, and show a conformational rearrangement upon calcium binding. This rearrangement involves, in particular, the hinge loop connecting the N-terminal and the C-terminal EF-hand domains, the reorientation of helix III with respect to helix IV, as common to several S100 proteins, and the elongation of helix IV. The details of the structural changes are important because they must be related to the different functions, still largely unknown, of the different members of the S100 family. For the first time for a full-length S100 protein, relaxation measurements were performed on both the apo and the calcium-bound forms. A quite large mobility was observed in the hinge loop, which is not quenched in the calcium form. The structural differences resulting upon calcium binding change the global shape and the distribution of hydrophobic and charged residues of the S100A5 homodimer in a modest but significantly different manner with respect to the closest homologues S100A4 and S100A6.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21046186 E.Babini, I.Bertini, V.Borsi, V.Calderone, X.Hu, C.Luchinat, and G.Parigi (2011).
Structural characterization of human S100A16, a low-affinity calcium binder.
  J Biol Inorg Chem, 16, 243-256.
PDB codes: 2l50 2l51 3nxa
21296671 M.Nowakowski, L.Jaremko, M.Jaremko, I.Zhukov, A.Belczyk, A.BierzyƄski, and A.Ejchart (2011).
Solution NMR structure and dynamics of human apo-S100A1 protein.
  J Struct Biol, 174, 391-399.
PDB code: 2l0p
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