1TLI

THERMOLYSIN (2% ISOPROPANOL SOAKED CRYSTALS)

Summary for 1TLI

• Entry DOI: 10.2210/pdb1tli/pdb
• Descriptor: THERMOLYSIN, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase, metalloproteinase, organic solvent
• Biological source: Bacillus thermoproteolyticus
• Cellular location: Secreted: P00800
• Total number of polymer chains: 1
• Total formula weight: 34666.16

Authors

English, A.C.,Done, S.H.,Groom, C.R.,Hubbard, R.E. (deposition date: 1998-10-27, release date: 2000-02-18, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.05 Å)