6J7N

Crystal structure of toxin TglT (unusual type guanylyltransferase-like toxin, Rv1045) mutant D82A co-expressed with TakA from Mycobacterium tuberculosis

6J7N の概要

• エントリーDOI: 10.2210/pdb6j7n/pdb
• 分子名称: guanylyltransferase-like toxin, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: guanylyltransferase;guanylyltransferase-like toxin;ta, toxin
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34497.28

構造登録者

Yu, X.,Gao, X.,Zhu, K.,Wojdyla, J.A.,Wang, M.,Cui, S. (登録日: 2019-01-18, 公開日: 2020-05-13, 最終更新日: 2023-11-22)

主引用文献

Yu, X.,Gao, X.,Zhu, K.,Yin, H.,Mao, X.,Wojdyla, J.A.,Qin, B.,Huang, H.,Wang, M.,Sun, Y.C.,Cui, S.
Characterization of a toxin-antitoxin system in Mycobacterium tuberculosis suggests neutralization by phosphorylation as the antitoxicity mechanism.
Commun Biol, 3:216-216, 2020

PubMed Abstract: Mycobacterium tuberculosis (Mtb) encodes an exceptionally large number of toxin-antitoxin (TA) systems, supporting the hypothesis that TA systems are involved in pathogenesis. We characterized the putative Mtb Rv1044-Rv1045 TA locus structurally and functionally, demonstrating that it constitutes a bona fide TA system but adopts a previously unobserved antitoxicity mechanism involving phosphorylation of the toxin. While Rv1045 encodes the guanylyltransferase TglT functioning as a toxin, Rv1044 encodes the novel atypical serine protein kinase TakA, which specifically phosphorylates the cognate toxin at residue S78, thereby neutralizing its toxicity. In contrast to previous predictions, we found that Rv1044-Rv1045 does not belong to the type IV TA family because TglT and TakA interact with each other as substrate and kinase, suggesting an unusual type of TA system. Protein homology analysis suggests that other COG5340-DUF1814 protein pairs, two highly associated but uncharacterized protein families widespread in prokaryotes, might share this unusual antitoxicity mechanism.

PubMed: 32382148
DOI: 10.1038/s42003-020-0941-1

実験手法

X-RAY DIFFRACTION (2.294 Å)