1SUB

CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN

1SUB の概要

• エントリーDOI: 10.2210/pdb1sub/pdb
• 分子名称: SUBTILISIN BPN' CRB-S3, CALCIUM ION, POTASSIUM ION, ... (5 entities in total)
• 機能のキーワード: hydrolase(serine proteinase)
• 由来する生物種: Bacillus amyloliquefaciens
• 細胞内の位置: Secreted: P00782
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27710.82

構造登録者

Gallagher, T.,Bryan, P.,Gilliland, G.L. (登録日: 1992-06-10, 公開日: 1994-01-31, 最終更新日: 2024-10-09)

主引用文献

Gallagher, T.,Bryan, P.,Gilliland, G.L.
Calcium-independent subtilisin by design.
Proteins, 16:205-213, 1993

PubMed Abstract: A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.

PubMed: 8332608
DOI: 10.1002/prot.340160207

実験手法

X-RAY DIFFRACTION (1.75 Å)