Tricorn protease - The core of a modular proteolytic system

被引：87

作者：

Tamura, T ^{[1
]}

Tamura, N ^{[1
]}

Cejka, Z ^{[1
]}

Hegerl, R ^{[1
]}

Lottspeich, F ^{[1
]}

Baumeister, W ^{[1
]}

机构：

[1] MAX PLANCK INST BIOCHEM, D-82152 MARTINSRIED, GERMANY

来源：

SCIENCE | 1996年 / 274卷 / 5291期

关键词：

D O I：

10.1126/science.274.5291.1385

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.

引用

页码：1385 / 1389

页数：5

共 31 条

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