期刊
CELL CALCIUM
卷 87, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.ceca.2020.102185
关键词
S100G; Calmodulin; Calcium sensor; EF-hand; Intrinsic disorder
类别
资金
- Russian Scientific Foundation [19-14-00289]
- Russian Science Foundation [19-14-00289] Funding Source: Russian Science Foundation
Bovine S100 G (calbindin D-9k, small Ca2+-binding protein of the EF-hand superfamily) is considered as a calcium buffer protein; i.e., the binding of Ca2+ practically does not change its general conformation. A set of experimental approaches has been used to study structural properties of apo- and Ca2+ -loaded forms of mouse S100 G (81.4% identity in amino acid sequence with bovine S100 G). This analysis revealed that, in contrast to bovine S100 G, the removal of calcium ions increases a-helices content of mouse S100 G protein and enhances its accessibility to digestion by alpha-chyrnotrypsin. Furthermore, mouse apo-S100 G is characterized by a decreased surface hydrophobicity and reduced tendency for oligomerization. Such behavior is typical of calcium sensor proteins. Apo-state of mouse S100 G still has rather compact structure, which can be cooperatively unfolded by temperature and GdnHCl. Computational analysis of amino acid sequences of S100 G proteins shows that these proteins could be in a disordered state upon a removal of the bound calcium ions. The experimental data show that, although mouse apo-S100 G is flexible compared to the Ca2+-loaded state, the apo-form is not completely disordered and preserves some cooperatively meting structure. The origin of the unexpectedly high stability of mouse S100 G can be rationalized by an exceptionally strong association of its N- and C-terminal parts containing the EF-hands I and II, respectively.
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