4DUQ

The Structure of Ca2+-loaded S100A2 at 1.3A resolution

「3N22」から置き換えられました

4DUQ の概要

• エントリーDOI: 10.2210/pdb4duq/pdb
• 分子名称: Protein S100-A2, CALCIUM ION, POLYETHYLENE GLYCOL (N=34), ... (4 entities in total)
• 機能のキーワード: ef-hand, calcium-binding, zinc-binding, tumor supressor, 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: 25381.08

構造登録者

Koch, M.,Fritz, G. (登録日: 2012-02-22, 公開日: 2012-03-07, 最終更新日: 2024-02-28)

主引用文献

Koch, M.,Fritz, G.
The structure of Ca2+-loaded S100A2 at 1.3- angstrom resolution.
Febs J., 279:1799-1810, 2012

PubMed Abstract: S100A2 is an EF-hand calcium ion (Ca(2+))-binding protein that activates the tumour suppressor p53. In order to understand the molecular mechanisms underlying the Ca(2+) -induced activation of S100A2, the structure of Ca(2+)-bound S100A2 was determined at 1.3 Å resolution by X-ray crystallography. The structure was compared with Ca(2+) -free S100A2 and with other S100 proteins. Binding of Ca(2+) to S100A2 induces small structural changes in the N-terminal EF-hand, but a large conformational change in the C-terminal EF-hand, reorienting helix III by approximately 90°. This movement is accompanied by the exposure of a hydrophobic cavity between helix III and helix IV that represents the target protein interaction site. This molecular reorganization is associated with the breaking and new formation of intramolecular hydrophobic contacts. The target binding site exhibits unique features; in particular, the hydrophobic cavity is larger than in other Ca(2+)-loaded S100 proteins. The structural data underline that the shape and size of the hydrophobic cavity are major determinants for target specificity of S100 proteins and suggest that the binding mode for S100A2 is different from that of other p53-interacting S100 proteins. Database Structural data are available in the Protein Data Bank database under the accession number 4DUQ

PubMed: 22394450
DOI: 10.1111/j.1742-4658.2012.08556.x

実験手法

X-RAY DIFFRACTION (1.3 Å)