1GXW

the 2.2 A resolution structure of thermolysin crystallized in presence of potassium thiocyanate

Summary for 1GXW

• Entry DOI: 10.2210/pdb1gxw/pdb
• Related: 1FJ3 1FJO 1FJQ 1FJT 1FJU 1FJV 1FJW 1HYT 1LNA 1LNB 1LNC 1LND 1LNE 1LNF 1QF0 1QF1 1QF2 1THL 1TLI 1TLP 1TLX 1TMN 1TRL 2TLI 2TLX 2TMN 3TLI 3TMN 4TLI 4TLN 4TMN 5TLI 5TLN 5TMN 6TLI 6TMN 7TLI 7TLN 8TLI 8TLN
• Descriptor: THERMOLYSIN, VALINE, LYSINE, ... (7 entities in total)
• Functional Keywords: hydrolase, thermolysin, metalloendopeptidase, thiocyanate, salting-in, metalloprotease
• Biological source: BACILLUS THERMOPROTEOLYTICUS
• Total number of polymer chains: 1
• Total formula weight: 34910.45

Authors

Gaucher, J.F.,Selkti, M.,Prange, T.,Tomas, A. (deposition date: 2002-04-12, release date: 2002-12-05, Last modification date: 2023-12-13)

Primary citation

Gaucher, J.,Selkti, M.,Prange, T.,Tomas, A.
The 2.2 A Resolution Structure of Thermolysin (Tln) Crystallized in the Presence of Potassium Thiocyanate.
Acta Crystallogr.,Sect.D, 58:2198-, 2002

PubMed Abstract: A new crystallization protocol for thermolysin (EC 3.4.24.27) from Bacillus thermoproteolyticus is presented. After dissolving the protein in the presence of KSCN, which avoids the use of DMSO and CsCl, crystals were obtained following the salting-in method. Crystal cell parameters are isomorphous with those previously reported from DMSO/CsCl mixtures. The new SCN(-) crystal structure has been analyzed. It shows the presence of one thiocyanate ion in the catalytic site and several rearrangements in the S(1) and S(2) subsites. These results are in agreement with the measurements of Inouye et al. [(1998), J. Biochem. (Tokyo), 123, 847-852], who observed in solution that the solubility of TLN, which is particularly poor in low ionic strength solutions, increases dramatically in the presence of several neutral salts. The results reported here suggest possible explanations for the solubility increase and for the inhibitory effects of high SCN(-) concentrations on thermolysin activity.

PubMed: 12454500
DOI: 10.1107/S0907444902015457

Experimental method

X-RAY DIFFRACTION (2.18 Å)