6TLI

THERMOLYSIN (60% ISOPROPANOL SOAKED CRYSTALS)

6TLI の概要

• エントリーDOI: 10.2210/pdb6tli/pdb
• 関連するPDBエントリー: 1TLI 1TLX 2TLI 2TLX 3TLI 4TLI 5TLI 7TLI 8TLI
• 分子名称: PROTEIN (THERMOLYSIN), ZINC ION, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, metalloproteinase, organic solvent
• 由来する生物種: Bacillus thermoproteolyticus
• 細胞内の位置: Secreted: P00800
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34846.44

構造登録者

English, A.C.,Done, S.H.,Groom, C.R.,Hubbard, R.E. (登録日: 1998-10-29, 公開日: 2000-03-13, 最終更新日: 2023-12-27)

主引用文献

English, A.C.,Done, S.H.,Caves, L.S.,Groom, C.R.,Hubbard, R.E.
Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol.
Proteins, 37:628-640, 1999

PubMed Abstract: Multiple-solvent crystal structure determination (MSCS) allows the position and orientation of bound solvent fragments to be identified by determining the structure of protein crystals soaked in organic solvents. We have extended this technique by the determination of high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 2% to 100% isopropanol. The procedure causes only minor changes to the conformation of the protein, and an increasing number of isopropanol interaction sites could be identified as the solvent concentration is increased. Isopropanol occupies all four of the main subsites in the active site, although this was only observed at very high concentrations of isopropanol for three of the four subsites. Analysis of the isopropanol positions shows little correlation with interaction energy computed using a molecular mechanics force field, but the experimentally determined positions of isopropanol are consistent with the structures of known protein-ligand complexes of TLN.

PubMed: 10651278
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<628::AID-PROT13>3.3.CO;2-7

実験手法

X-RAY DIFFRACTION (2.1 Å)