9B78

Mycobacterium tuberculosis CoaX Homohexamer

9B78 の概要

• エントリーDOI: 10.2210/pdb9b78/pdb
• EMDBエントリー: 44303
• 分子名称: Type III pantothenate kinase (1 entity in total)
• 機能のキーワード: pantothenate kinase isoform, cytosolic protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 176050.07

構造登録者

Chen, J.,Ekiert, D.C.,Bhabha, G. (登録日: 2024-03-27, 公開日: 2024-11-13, 最終更新日: 2024-12-11)

主引用文献

Kahne, S.C.,Yoo, J.H.,Chen, J.,Nakedi, K.,Iyer, L.M.,Putzel, G.,Samhadaneh, N.M.,Pironti, A.,Aravind, L.,Ekiert, D.C.,Bhabha, G.,Rhee, K.Y.,Darwin, K.H.
Identification of a depupylation regulator for an essential enzyme in Mycobacterium tuberculosis.
Proc.Natl.Acad.Sci.USA, 121:e2407239121-e2407239121, 2024

PubMed Abstract: In , proteins that are posttranslationally modified with a prokaryotic ubiquitin-like protein (Pup) can be degraded by bacterial proteasomes. A single Pup-ligase and depupylase shape the pupylome, but the mechanisms regulating their substrate specificity are incompletely understood. Here, we identified a depupylation regulator, a protein called CoaX, through its copurification with the depupylase Dop. CoaX is a pseudopantothenate kinase that showed evidence of binding to pantothenate, an essential nutrient synthesizes, but not its phosphorylation. In a ∆ mutant, pantothenate synthesis enzymes including PanB, a substrate of the Pup-proteasome system (PPS), were more abundant than in the parental strain. In vitro, CoaX specifically accelerated depupylation of Pup~PanB, while addition of pantothenate inhibited this reaction. In culture, media supplementation with pantothenate decreased PanB levels, which required CoaX. Collectively, we propose CoaX regulates PanB abundance in response to pantothenate levels by modulating its vulnerability to proteolysis by proteasomes.

PubMed: 39585979
DOI: 10.1073/pnas.2407239121

実験手法

ELECTRON MICROSCOPY (2.59 Å)