1T1E

High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)

1T1E の概要

• エントリーDOI: 10.2210/pdb1t1e/pdb
• 関連するPDBエントリー: 1GT9 1GTG 1GTJ 1GTL 1T1G 1T1I
• 分子名称: kumamolisin, CALCIUM ION (3 entities in total)
• 機能のキーワード: proenzyme, prosubtilase, activation mechanism, sedolisin, serine-carboxyl proteinase, hydrolase
• 由来する生物種: Bacillus sp. MN-32
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57788.97

構造登録者

Comellas-Bigler, M.,Maskos, K.,Huber, R.,Oyama, H.,Oda, K.,Bode, W. (登録日: 2004-04-16, 公開日: 2004-08-03, 最終更新日: 2024-04-03)

主引用文献

Comellas-Bigler, M.,Maskos, K.,Huber, R.,Oyama, H.,Oda, K.,Bode, W.
1.2 a crystal structure of the serine carboxyl proteinase pro-kumamolisin: structure of an intact pro-subtilase
Structure, 12:1313-1323, 2004

PubMed Abstract: Kumamolisin, an extracellular proteinase derived from an acido/thermophilic Bacillus, belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad. In kumamolisin, the Asp82 carboxylate hydrogen bonds to Glu32-Trp129, which might act as a proton sink stabilizing the catalytic residues. The 1.2/1.3 A crystal structures of the Glu32-->Ala and Trp129-->Ala mutants show that both mutations affect the active-site conformation, causing a 95% activity decrease. In addition, the 1.2 A crystal structure of the Ser278-->Ala mutant of pro-kumamolisin was determined. The prodomain exhibits a half-beta sandwich core docking to the catalytic domain similarly as the equivalent subtilisin prodomains in their catalytic-domain complexes. This pro-kumamolisin structure displays, for the first time, the uncleaved linker segment running across the active site and connecting the prodomain with the properly folded catalytic domain. The structure strongly points to an initial intramolecular activation cleavage in subtilases, as presumed for pro-subtilisin and pro-furin.

PubMed: 15242607
DOI: 10.1016/j.str.2004.04.013

実験手法

X-RAY DIFFRACTION (1.18 Å)