3OUK

Crystal structure of Rv3910 from Mycobacterium Tuberculosis

3OUK の概要

• エントリーDOI: 10.2210/pdb3ouk/pdb
• 関連するPDBエントリー: 3OTV 3OUN 3UQC
• 分子名称: PROBABLE CONSERVED TRANSMEMBRANE PROTEIN (2 entities in total)
• 機能のキーワード: peptidoglycan, ser/thr kinase, pseudokinase, regulation, membrane protein, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30133.94

構造登録者

Gee, C.L.,Alber, T. (登録日: 2010-09-15, 公開日: 2012-02-08, 最終更新日: 2024-04-03)

主引用文献

Gee, C.L.,Papavinasasundaram, K.G.,Blair, S.R.,Baer, C.E.,Falick, A.M.,King, D.S.,Griffin, J.E.,Venghatakrishnan, H.,Zukauskas, A.,Wei, J.R.,Dhiman, R.K.,Crick, D.C.,Rubin, E.J.,Sassetti, C.M.,Alber, T.
A phosphorylated pseudokinase complex controls cell wall synthesis in mycobacteria
Sci.Signal., 5:ra7-ra7, 2012

PubMed Abstract: Prokaryotic cell wall biosynthesis is coordinated with cell growth and division, but the mechanisms regulating this dynamic process remain obscure. Here, we describe a phosphorylation-dependent regulatory complex that controls peptidoglycan (PG) biosynthesis in Mycobacterium tuberculosis. We found that PknB, a PG-responsive Ser-Thr protein kinase (STPK), initiates complex assembly by phosphorylating a kinase-like domain in the essential PG biosynthetic protein, MviN. This domain was structurally diverged from active kinases and did not mediate phosphotransfer. Threonine phosphorylation of the pseudokinase domain recruited the FhaA protein through its forkhead-associated (FHA) domain. The crystal structure of this phosphorylated pseudokinase-FHA domain complex revealed the basis of FHA domain recognition, which included unexpected contacts distal to the phosphorylated threonine. Conditional degradation of these proteins in mycobacteria demonstrated that MviN was essential for growth and PG biosynthesis and that FhaA regulated these processes at the cell poles and septum. Controlling this spatially localized PG regulatory complex is only one of several cellular roles ascribed to PknB, suggesting that the capacity to coordinate signaling across multiple processes is an important feature conserved between eukaryotic and prokaryotic STPK networks.

PubMed: 22275220
DOI: 10.1126/scisignal.2002525

実験手法

X-RAY DIFFRACTION (3.402 Å)