1NLU

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

1NLU の概要

• エントリーDOI: 10.2210/pdb1nlu/pdb
• 関連するPDBエントリー: 1ga6 1kdv
• 関連するBIRD辞書のPRD_ID: PRD_000754
• 分子名称: SEDOLISIN, PSEUDO-IODOTYROSTATIN, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: pscp, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Pseudomonas sp.; 詳細
• 細胞内の位置: Periplasm: P42790
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 39335.83

構造登録者

Wlodawer, A.,Li, M.,Gustchina, A.,Dauter, Z.,Uchida, K.,Oyama, H.,Glodfarb, N.E.,Dunn, B.M.,Oda, K. (登録日: 2003-01-07, 公開日: 2004-01-20, 最終更新日: 2025-03-26)

主引用文献

Wlodawer, A.,Li, M.,Gustchina, A.,Oyama, H.,Oda, K.,Beyer, B.B.,Clemente, J.,Dunn, B.M.
Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate.
Biochem.Biophys.Res.Commun., 314:638-645, 2004

PubMed Abstract: High-resolution crystallographic analysis of a complex of the serine-carboxyl proteinase sedolisin with pseudo-iodotyrostatin revealed two molecules of this inhibitor bound in the active site of the enzyme, marking subsites from S3 to S3('). The mode of binding represents two products of the proteolytic reaction. Substrate specificity of sedolisin was investigated using peptide libraries and a new peptide substrate for sedolisin, MCA-Lys-Pro-Pro-Leu-Glu#Tyr-Arg-Leu-Gly-Lys(DNP)-Gly, was synthesized based on the results of the enzymatic and crystallographic studies and was shown to be efficiently cleaved by the enzyme. The kinetic parameters for the substrate, measured by the increase in fluorescence upon relief of quenching, were: k(cat)=73+/-5 s(-1), K(m)=0.12+/-0.011 microM, and k(cat)/K(m)=608+/-85 s(-1)microM(-1).

PubMed: 14733955
DOI: 10.1016/j.bbrc.2003.12.130

実験手法

X-RAY DIFFRACTION (1.3 Å)