1S2N

Crystal structure of a cold adapted subtilisin-like serine proteinase

1S2N の概要

• エントリーDOI: 10.2210/pdb1s2n/pdb
• 分子名称: extracellular subtilisin-like serine proteinase, CALCIUM ION, phenylmethanesulfonic acid, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Vibrio sp. PA-44
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58589.66

構造登録者

Arnorsdottir, J.,Kristjansson, M.M.,Ficner, R. (登録日: 2004-01-09, 公開日: 2005-02-22, 最終更新日: 2024-11-06)

主引用文献

Arnorsdottir, J.,Kristjansson, M.M.,Ficner, R.
Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation.
FEBS J., 272:832-845, 2005

PubMed Abstract: The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be determined and its elucidation facilitates examination of the molecular principles underlying temperature adaptation in enzymes. The cold-adapted Vibrio proteinase was compared with known three-dimensional structures of homologous enzymes of meso- and thermophilic origin, proteinase K and thermitase, to which it has high structural resemblance. The main structural features emerging as plausible determinants of temperature adaptation in the enzymes compared involve the character of their exposed and buried surfaces, which may be related to temperature-dependent variation in the physical properties of water. Thus, the hydrophobic effect is found to play a significant role in the structural stability of the meso- and thermophile enzymes, whereas the cold-adapted enzyme has more of its apolar surface exposed. In addition, the cold-adapted Vibrio proteinase is distinguished from the more stable enzymes by its strong anionic character arising from the high occurrence of uncompensated negatively charged residues at its surface. Interestingly, both the cold-adapted and thermophile proteinases differ from the mesophile enzyme in having more extensive hydrogen- and ion pair interactions in their structures; this supports suggestions of a dual role of electrostatic interactions in the adaptation of enzymes to both high and low temperatures. The Vibrio proteinase has three calcium ions associated with its structure, one of which is in a calcium-binding site not described in other subtilases.

PubMed: 15670163
DOI: 10.1111/j.1742-4658.2005.04523.x

実験手法

X-RAY DIFFRACTION (2.44 Å)