Gupta, Arvind Kumar and Behera, Debashree and Gopal, Balasubramanian (2018) The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism. In: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 74 (12). pp. 803-809.
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Abstract
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.
Item Type: | Journal Article |
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Publication: | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS |
Publisher: | INT UNION CRYSTALLOGRAPHY |
Additional Information: | Copyright for this article belongs to INT UNION CRYSTALLOGRAPHY |
Keywords: | regulated proteolysis; high-temperature requirement A protein; PDZ domain; Mycobacterium tuberculosis |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 22 Jan 2019 17:08 |
Last Modified: | 22 Jan 2019 17:08 |
URI: | http://eprints.iisc.ac.in/id/eprint/61373 |
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