3TMN

THE BINDING OF L-VALYL-L-TRYPTOPHAN TO CRYSTALLINE THERMOLYSIN ILLUSTRATES THE MODE OF INTERACTION OF A PRODUCT OF PEPTIDE HYDROLYSIS

3TMN の概要

• エントリーDOI: 10.2210/pdb3tmn/pdb
• 分子名称: THERMOLYSIN, VALINE, TRYPTOPHAN, ... (6 entities in total)
• 機能のキーワード: hydrolase, metalloproteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 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: 34909.40

構造登録者

Holden, H.M.,Matthews, B.W. (登録日: 1987-06-29, 公開日: 1989-01-09, 最終更新日: 2024-05-22)

主引用文献

Holden, H.M.,Matthews, B.W.
The binding of L-valyl-L-tryptophan to crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis.
J.Biol.Chem., 263:3256-3260, 1988

PubMed Abstract: Crystallographic analysis of the binding of mercaptoacetyl-L-valyl-L-tryptophan to thermolysin suggests that this inhibitor is hydrolyzed by the crystalline enzyme. The apparent product of hydrolysis, L-valyl-L-tryptophan (Val-Trp), occupies the S1'-S2' subsites of the active site, not the S1-S1' subsites as observed previously for the dipeptide L-alanyl-L-phenylalanine (Ala-Phe). The difference in binding of Val-Trp and Ala-Phe is consistent with the specificity requirements and preferences of thermolysin. The binding of Val-Trp illustrates the mode of interaction of one of the products of peptide hydrolysis. High resolution crystallographic refinement indicates that the valyl amino group makes three hydrogen bonds to the enzyme and to solvent and, in addition, is 2.8 A from the carboxylate of Glu-143. This is the first instance in which a direct interaction has been observed between Glu-143 and the scissile nitrogen. As such, the study directly supports the mechanism of action for thermolysin proposed by Hangauer et al. (Hangauer, D. G., Monzingo, A. F., and Matthews, B. W. (1984) Biochemistry 23, 5730-5741) and, by analogy, indirectly supports the similar mechanism proposed for carboxypeptidase A (Monzingo, A. F., and Matthews, B. W. (1984) Biochemistry 23, 5724-5729).

PubMed: 3343246

実験手法

X-RAY DIFFRACTION (1.7 Å)