6IEO
Crystal structure of Mycobacterium tuberculosis HtrA1 (Rv1223) in regulated conformation
Summary for 6IEO
| Entry DOI | 10.2210/pdb6ieo/pdb |
| Descriptor | Probable serine protease HtrA (DEGP protein), phenylmethanesulfonic acid (3 entities in total) |
| Functional Keywords | hydrolase, htra family of serine protease, chymotrypsin like, periplasm, protein quality control and signal transduction, membrane protein |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 1 |
| Total formula weight | 32694.59 |
| Authors | Gupta, A.K.,Gopal, B. (deposition date: 2018-09-14, release date: 2018-12-19, Last modification date: 2024-10-30) |
| Primary citation | Gupta, A.K.,Behera, D.,Gopal, B. The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism. Acta Crystallogr F Struct Biol Commun, 74:803-809, 2018 Cited by PubMed 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. PubMed: 30511675DOI: 10.1107/S2053230X18016217 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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