1MRU

Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB.

1MRU の概要

• エントリーDOI: 10.2210/pdb1mru/pdb
• 分子名称: Probable serine/threonine-protein kinase pknB, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: regulatory, atp-recognition, molecular evolution, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68181.07

構造登録者

Young, T.A.,Delagoutte, B.,Endrizzi, J.A.,Alber, T.,TB Structural Genomics Consortium (TBSGC) (登録日: 2002-09-18, 公開日: 2003-02-11, 最終更新日: 2024-02-14)

主引用文献

Young, T.A.,Delagoutte, B.,Endrizzi, J.A.,Falick, A.M.,Alber, T.
Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases.
Nat.Struct.Biol., 10:168-174, 2003

PubMed Abstract: A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins. Here we characterize PknB, a transmembrane signaling kinase from Mycobacterium tuberculosis. The intracellular PknB kinase domain is active autonomously, and the active enzyme is phosphorylated on residues homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases. The crystal structure of the PknB kinase domain in complex with an ATP analog reveals the active conformation. The predicted fold of the PknB extracellular domain matches the proposed targeting domain of penicillin-binding protein 2x. The structural and chemical similarities of PknB to metazoan homologs support a universal activation mechanism of Ser/Thr protein kinases in prokaryotes and eukaryotes.

PubMed: 12548283
DOI: 10.1038/nsb897

実験手法

X-RAY DIFFRACTION (3 Å)