Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 378, Issue 4, Pages 933-942Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.03.019
Keywords
S100A2; EF hand; X-ray structure; calcium; sodium
Categories
Ask authors/readers for more resources
S100A2 is an EF hand-containing Ca2+-binding protein of the family of S100 proteins. The protein is localized exclusively in the nucleus and is involved in cell cycle regulation. It attracted most interest by its function as a tumor suppressor via p53 interaction. We determined the crystal structure of homodimeric S100A2 in the Ca2+-free state at 1.6-angstrom resolution. The structure revealed structural differences between subunits A and B, especially in the conformation of a loop that connects the N- and C-terminal EF hands and represents a part of the target-binding site in S100 proteins. Analysis of the hydrogen bonding network and molecular dynamics calculations indicate that one of the two observed conformations is more stable. The structure revealed Na+ bound to each N-terminal EF hand of both subunits coordinated by oxygen atoms of the backbone carbonyl and water molecules. Comparison with the structures of Ca2+-free S100A3 and S100A6 suggests that Na+ might occupy the S100-specific EF hand in the Ca2+-free state. (c) 2008 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available