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From Proteopedia
Crystal structure of Mycobacterium tuberculosis HtrA1 (Rv1223) in regulated conformation
Structural highlights
FunctionHTRA1_MYCTU Essential protein that may act as a regulatory protease that is conditionally activated upon appropriate environmental triggers.[1] Publication Abstract from PubMedThe crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein was determined at 1.83 A 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. The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism.,Gupta AK, Behera D, Gopal B Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):803-809. doi:, 10.1107/S2053230X18016217. Epub 2018 Nov 29. PMID:30511675[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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