2KUI

NMR structure of the PASTA domain of Mycobacterium tuberculosis of PknB

2KUI の概要

• エントリーDOI: 10.2210/pdb2kui/pdb
• 関連するPDBエントリー: 2KUD 2KUE 2KUF
• 分子名称: Serine/threonine-protein kinase pknB (1 entity in total)
• 機能のキーワード: kinase, external domain, signaling, stpk, resuscitation, serine/threonine-protein kinase, 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: 28777.09

構造登録者

Barthe, P.,Mukamolova, G.,Roumestand, C.,Cohen-Gonsaud, M. (登録日: 2010-02-17, 公開日: 2010-04-14, 最終更新日: 2024-05-29)

主引用文献

Barthe, P.,Mukamolova, G.V.,Roumestand, C.,Cohen-Gonsaud, M.
The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation
Structure, 18:606-615, 2010

PubMed Abstract: PknB is a transmembrane Ser/Thr protein kinase that defines and belongs to an ultraconserved kinase subfamily found in Gram-positive bacteria. Essential for Mycobacterium tuberculosis growth, its close homolog in Bacillus subtilis has been linked to exit from dormancy. The kinase possesses an extracellular region composed of a repetition of PASTA domains, believed to bind peptidoglycan fragments that might act as a signaling molecule. We report here the first solution structure of this extracellular region. Small-angle X-ray scattering and nuclear magnetic resonance studies show that the four PASTA domains display an unexpected linear organization, contrary to what is observed in the distant protein PBP2x from Streptococccus pneumoniae where two PASTA domains fold over in a compact structure. We propose a model for PknB activation based on a ligand-dependent dimerization of the extracellular PASTA domains that initiates multiple signaling pathways.

PubMed: 20462494
DOI: 10.1016/j.str.2010.02.013

実験手法

SOLUTION NMR