1SCB

ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT

1SCB の概要

• エントリーDOI: 10.2210/pdb1scb/pdb
• 分子名称: SUBTILISIN CARLSBERG, CALCIUM ION, ACETONITRILE, ... (4 entities in total)
• 機能のキーワード: serine protease
• 由来する生物種: Bacillus licheniformis
• 細胞内の位置: Secreted: P00780
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27838.90

構造登録者

Fitzpatrick, P.A.,Steinmetz, A.C.U.,Ringe, D.,Klibanov, A.M. (登録日: 1993-07-13, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Fitzpatrick, P.A.,Steinmetz, A.C.,Ringe, D.,Klibanov, A.M.
Enzyme crystal structure in a neat organic solvent.
Proc.Natl.Acad.Sci.USA, 90:8653-8657, 1993

PubMed Abstract: The crystal structure of the serine protease subtilisin Carlsberg in anhydrous acetonitrile was determined at 2.3 A resolution. It was found to be essentially identical to the three-dimensional structure of the enzyme in water; the differences observed were smaller than those between two independently determined structures in aqueous solution. The hydrogen bond system of the catalytic triad is intact in acetonitrile. The majority (99 of 119) of enzyme-bound, structural water molecules have such a great affinity to subtilisin that they are not displaced even in anhydrous acetonitrile. Of the 12 enzyme-bound acetonitrile molecules, 4 displace water molecules and 8 bind where no water had been observed before. One-third of all subtilisin-bound acetonitrile molecules reside in the active center, occupying the same region (P1, P2, and P3 binding sites) as the specific protein inhibitor eglin c.

PubMed: 8378343
DOI: 10.1073/pnas.90.18.8653

実験手法

X-RAY DIFFRACTION (2.3 Å)