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8YPJ

Cyrstal structure of the MazE-mt10 Antitoxin from Mycobacterium tuberculosis

Summary for 8YPJ
Entry DOI10.2210/pdb8ypj/pdb
DescriptorAntitoxin, PHOSPHATE ION (3 entities in total)
Functional Keywordsantitoxin, maze, mycobacterium tuberculosis, dna binding, signaling protein
Biological sourceMycobacterium tuberculosis
Total number of polymer chains2
Total formula weight16377.37
Authors
Lee, K.Y. (deposition date: 2024-03-17, release date: 2024-05-15)
Primary citationEun, H.J.,Lee, S.Y.,Lee, K.Y.
DNA binding reveals hidden interdomain allostery of a MazE antitoxin from Mycobacterium tuberculosis.
Biochem.Biophys.Res.Commun., 710:149898-149898, 2024
Cited by
PubMed Abstract: Type II toxin-antitoxin (TA) systems are ubiquitously distributed genetic elements in prokaryotes and are crucial for cell maintenance and survival under environmental stresses. The antitoxin is a modular protein consisting of the disordered C-terminal region that physically contacts and neutralizes the cognate toxin and the well-folded N-terminal DNA binding domain responsible for autorepression of TA transcription. However, how the two functional domains communicate is largely unknown. Herein, we determined the crystal structure of the N-terminal domain of the type II antitoxin MazE-mt10 from Mycobacterium tuberculosis, revealing a homodimer of the ribbon-helix-helix (RHH) fold with distinct DNA binding specificity. NMR studies demonstrated that full-length MazE-mt10 forms the helical and coiled states in equilibrium within the C-terminal region, and that helical propensity is allosterically enhanced by the N-terminal binding to the cognate operator DNA. This coil-to-helix transition may promote toxin binding/neutralization of MazE-mt10 and further stabilize the TA-DNA transcription repressor. This is supported by many crystal structures of type II TA complexes in which antitoxins form an α-helical structure at the TA interface. The hidden helical state of free MazE-mt10 in solution, favored by DNA binding, adds a new dimension to the regulatory mechanism of type II TA systems. Furthermore, complementary approaches using X-ray crystallography and NMR allow us to study the allosteric interdomain interplay of many other full-length antitoxins of type II TA systems.
PubMed: 38598903
DOI: 10.1016/j.bbrc.2024.149898
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.91 Å)
Structure validation

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数据于2024-11-06公开中

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