2RGI

Crystal structure of Ca2+-free S100A2 at 1.6 A resolution

2RGI の概要

• エントリーDOI: 10.2210/pdb2rgi/pdb
• 分子名称: Protein S100-A2, SODIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total)
• 機能のキーワード: alpha helical, ef-hand, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22258.05

構造登録者

Koch, M.,Diez, J.,Fritz, G. (登録日: 2007-10-03, 公開日: 2008-01-29, 最終更新日: 2023-08-30)

主引用文献

Koch, M.,Diez, J.,Fritz, G.
Crystal structure of Ca2+ -free S100A2 at 1.6-A resolution.
J.Mol.Biol., 378:931-940, 2008

PubMed Abstract: S100A2 is an EF hand-containing Ca(2+)-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 Ca(2+)-free state at 1.6-A 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 Ca(2+)-free S100A3 and S100A6 suggests that Na(+) might occupy the S100-specific EF hand in the Ca(2+)-free state.

PubMed: 18394645
DOI: 10.1016/j.jmb.2008.03.019

実験手法

X-RAY DIFFRACTION (1.6 Å)