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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
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Crystal structure study on human S100A13 at 2.0 A resolution.

Mei Li1, Ping-Feng Zhang, Xiao-Wei Pan

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. meili@moon.ibp.ac.cn

Biochemical and Biophysical Research Communications
|March 22, 2007
PubMed
Summary

The S100A13 protein, a calcium-binding protein, has a unique amphiphilic alpha-helix structure. This structure may explain its role in releasing signal peptide-less proteins like FGF-1.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The S100 protein family comprises over 25 calcium-binding proteins.
  • S100A13 is widely expressed and implicated in stress-induced protein release, inflammation, and angiogenesis.

Purpose of the Study:

  • To determine the crystal structure of the Ca(2+)-bound form of S100A13.
  • To elucidate the structural basis for S100A13's unique functions.

Main Methods:

  • X-ray crystallography was used to determine the structure of Ca(2+)-bound S100A13.
  • The resolution of the crystal structure was 2.0 Å.

Main Results:

  • S100A13 forms a homodimer with four EF-hand motifs.
  • A unique structural feature of S100A13 is that all its alpha-helices are amphiphilic.
  • This amphiphilic nature was not observed in other S100 members.

Conclusions:

  • The determined crystal structure provides insights into S100A13's molecular architecture.
  • The unique amphiphilic alpha-helix structure is proposed to be responsible for S100A13's function in mediating the release of proteins like FGF-1 and IL-1alpha.