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Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):803-809. doi: 10.1107/S2053230X18016217. Epub 2018 Nov 29.

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

Author information

1
Molecular Biophysics Unit, Indian Institute of Science, C. V. Raman Road, Bangalore 560 012, India.

Abstract

The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 Å 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.

KEYWORDS:

Mycobacterium tuberculosis; PDZ domain; high-temperature requirement A protein; regulated proteolysis

PMID:
30511675
DOI:
10.1107/S2053230X18016217
[Indexed for MEDLINE]

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