5XLM

Monomer form of M.tuberculosis PknI sensor domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.222 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural Insight into the Activation of PknI Kinase from M. tuberculosis via Dimerization of the Extracellular Sensor Domain.

Yan, Q.Jiang, D.Qian, L.Zhang, Q.Zhang, W.Zhou, W.Mi, K.Guddat, L.Yang, H.Rao, Z.

(2017) Structure 25: 1286-1294.e4

  • DOI: https://doi.org/10.1016/j.str.2017.06.010
  • Primary Citation of Related Structures:  
    5XKA, 5XLL, 5XLM

  • 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.


  • Organizational Affiliation

    College of Life Sciences, Nankai University, Tianjin 300071, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase PknI
A, B
214Mycobacterium tuberculosis H37RvMutation(s): 0 
Gene Names: pknIRv2914cMTCY338.02c
EC: 2.7.11.1
UniProt
Find proteins for P9WI69 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WI69 
Go to UniProtKB:  P9WI69
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WI69
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.256 
  • R-Value Work: 0.220 
  • R-Value Observed: 0.222 
  • Space Group: P 31
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.791α = 90
b = 58.791β = 90
c = 92.094γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Ministry of Science and TechnologyChina2014CB542800
National Natural Science Foundation of China (NSFC)China81330036
National Natural Science Foundation of China (NSFC)China81520108019

Revision History  (Full details and data files)

  • Version 1.0: 2018-05-16
    Type: Initial release
  • Version 1.1: 2021-10-27
    Changes: Author supporting evidence, Database references