JBIC Journal of Biological Inorganic Chemistry

, Volume 16, Issue 2, pp 243–256

Structural characterization of human S100A16, a low-affinity calcium binder

  • Elena Babini
  • Ivano Bertini
  • Valentina Borsi
  • Vito Calderone
  • Xiaoyu Hu
  • Claudio Luchinat
  • Giacomo Parigi
Original Paper

DOI: 10.1007/s00775-010-0721-3

Cite this article as:
Babini, E., Bertini, I., Borsi, V. et al. J Biol Inorg Chem (2011) 16: 243. doi:10.1007/s00775-010-0721-3

Abstract

The homodimeric structure of human S100A16 in the apo state has been obtained both in the solid state and in solution, resulting in good agreement between the structures with the exception of two loop regions. The homodimeric solution structure of human S100A16 was also calculated in the calcium(II)-bound form. Differently from most S100 proteins, the conformational rearrangement upon calcium binding is minor. This characteristic is likely to be related to the weak binding affinity of the protein for the calcium(II) ions. In turn, this is ascribed to the lack of the glutamate residue at the end of the S100-specific N-domain binding site, which in most S100 proteins provides two important side chain oxygen atoms as calcium(II) ligands. Furthermore, the presence of hydrophobic interactions stronger than for other S100 proteins, present in the closed form of S100A16 between the third and fourth helices, likely make the closed structure of the second EF-hand particularly stable, so even upon calcium(II) binding such a conformation is not disrupted.

Keywords

S100A16EF-hand proteinsCalcium-binding proteinsS100 proteinsProtein dynamics

Supplementary material

775_2010_721_MOESM1_ESM.pdf (120 kb)
Supplementary material 1 (PDF 120 kb)

Copyright information

© SBIC 2010

Authors and Affiliations

  • Elena Babini
    • 1
  • Ivano Bertini
    • 2
    • 3
  • Valentina Borsi
    • 2
  • Vito Calderone
    • 2
  • Xiaoyu Hu
    • 2
  • Claudio Luchinat
    • 2
    • 3
  • Giacomo Parigi
    • 2
    • 3
  1. 1.Department of Food ScienceUniversity of BolognaCesenaItaly
  2. 2.Magnetic Resonance Center (CERM)University of FlorenceSesto FiorentinoItaly
  3. 3.Department of ChemistryUniversity of FlorenceSesto FiorentinoItaly