5XLM

Monomer form of M.tuberculosis PknI sensor domain

5XLM の概要

• エントリーDOI: 10.2210/pdb5xlm/pdb
• 分子名称: Serine/threonine-protein kinase PknI (2 entities in total)
• 機能のキーワード: monomer, sensor domain, pkni, m.tuberculosis, transferase
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• 細胞内の位置: Cytoplasm : P9WI69
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45260.39

構造登録者

Rao, Z.,Yan, Q. (登録日: 2017-05-10, 公開日: 2018-05-16, 最終更新日: 2024-11-13)

主引用文献

Yan, Q.,Jiang, D.,Qian, L.,Zhang, Q.,Zhang, W.,Zhou, W.,Mi, K.,Guddat, L.,Yang, H.,Rao, Z.
Structural Insight into the Activation of PknI Kinase from M. tuberculosis via Dimerization of the Extracellular Sensor Domain.
Structure, 25:1286-1294.e4, 2017

PubMed Abstract: Protein kinases play central roles in the survival of Mycobacterium tuberculosis within host. Here we report the individual high-resolution crystal structures of the sensor domain (in both monomer and dimer forms) and the kinase domain of PknI, a transmembrane protein member of the serine/threonine protein kinases (STPKs) family. PknI is the first STPK identified whose sensor domain exists in a monomer-dimer equilibrium. Inspection of the two structures of the sensor domain (PknI_SD) revealed conformational changes upon dimerization, with an arm region of critical importance for dimer formation identified. Rapamycin-induced dimerization of unphosphorylated fusions of PknI juxtamembrane and the kinase domain, intended to mimic the dimerization effect presumably imposed by PknI_SD, was observed to be able to activate auto-phosphorylation activity of the kinase domain. In vivo experiments using an M. bovis model suggested PknI functions as a dimer in the regulation of M. tuberculosis growth.

PubMed: 28712808
DOI: 10.1016/j.str.2017.06.010

実験手法

X-RAY DIFFRACTION (2.2 Å)