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JBIC Journal of Biological Inorganic Chemistry

, Volume 14, Issue 7, pp 1097–1107 | Cite as

Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states

  • Ivano BertiniEmail author
  • Soumyasri Das Gupta
  • Xiaoyu Hu
  • Tilemachos Karavelas
  • Claudio Luchinat
  • Giacomo Parigi
  • Jing Yuan
Original Paper

Abstract

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.

Keywords

Calcium binding proteins Calcium-induced conformational rearrangements EF-hand proteins Protein dynamics S100A5 

Notes

Acknowledgments

This work was supported by Ente Cassa di Risparmio di Firenze, MIUR-FIRB contracts RBLA032ZM7 and RBIP06LSS2, and the European Commission, contracts EU-NMR 026145, SPINE2-COMPLEXES 031220, and LSHG-CT-2004-512052.

Supplementary material

775_2009_553_MOESM1_ESM.pdf (18 kb)
Supplementary Table S1 (PDF 18 kb)

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Copyright information

© SBIC 2009

Authors and Affiliations

  • Ivano Bertini
    • 1
    • 2
    Email author
  • Soumyasri Das Gupta
    • 1
  • Xiaoyu Hu
    • 1
  • Tilemachos Karavelas
    • 1
    • 3
  • Claudio Luchinat
    • 1
    • 4
  • Giacomo Parigi
    • 1
    • 4
  • Jing Yuan
    • 1
  1. 1.Magnetic Resonance Center (CERM)University of FlorenceSesto FiorentinoItaly
  2. 2.Department of ChemistryUniversity of FlorenceSesto FiorentinoItaly
  3. 3.Department of ChemistryUniversity of IoanninaIoanninaGreece
  4. 4.Department of Agricultural BiotechnologyUniversity of FlorenceFlorenceItaly

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