The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism

被引：2

作者：

Gupta, Arvind Kumar ^{[1
]}

Behera, Debashree ^{[1
]}

Gopal, Balasubramanian ^{[1
]}

机构：

[1] Indian Inst Sci, Mol Biophys Unit, CV Raman Rd, Bangalore 560012, Karnataka, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2018年 / 74卷

关键词：

regulated proteolysis; high-temperature requirement A protein; PDZ domain; Mycobacterium tuberculosis; DEGS STRESS-SENSOR; ATOMIC-RESOLUTION; INTEGRATION; PROTEASES; SIGNALS; RELIEF;

D O I：

10.1107/S2053230X18016217

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 angstrom resolution. This membrane-associated protease is essential for the survival of M. tuberculosis. The crystal structure reveals that interactions between the PDZ domain and the catalytic domain in HtrA lead to an inactive conformation. This finding is consistent with its proposed role as a regulatory protease that is conditionally activated upon appropriate environmental triggers. The structure provides a basis for directed studies to evaluate the role of this essential protein and the regulatory pathways that are influenced by this protease.

引用

页码：803 / 809

页数：7

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