6J73

Crystal structure of IniA from Mycobacterium smegmatis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.211 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.219 

wwPDB Validation 3D Report Full Report


This is version 1.0 of the entry. See complete history

Literature

Mycobacterial dynamin-like protein IniA mediates membrane fission.

Wang, M.Guo, X.Yang, X.Zhang, B.Ren, J.Liu, A.Ran, Y.Yan, B.Chen, F.Guddat, L.W.Hu, J.Li, J.Rao, Z.

(2019) Nat Commun 10: 3906-3906

  • DOI: 10.1038/s41467-019-11860-z
  • Primary Citation of Related Structures:  

  • PubMed Abstract: 
  • Mycobacterium tuberculosis infection remains a major threat to human health worldwide. Drug treatments against tuberculosis (TB) induce expression of several mycobacterial proteins, including IniA, but its structure and function remain poorly underst ...

    Mycobacterium tuberculosis infection remains a major threat to human health worldwide. Drug treatments against tuberculosis (TB) induce expression of several mycobacterial proteins, including IniA, but its structure and function remain poorly understood. Here, we report the structures of Mycobacterium smegmatis IniA in both the nucleotide-free and GTP-bound states. The structures reveal that IniA folds as a bacterial dynamin-like protein (BDLP) with a canonical GTPase domain followed by two helix-bundles (HBs), named Neck and Trunk. The distal end of its Trunk domain exists as a lipid-interacting (LI) loop, which binds to negatively charged lipids for membrane attachment. IniA does not form detectable nucleotide-dependent dimers in solution. However, lipid tethering indicates nucleotide-independent association of IniA on the membrane. IniA also deforms membranes and exhibits GTP-hydrolyzing dependent membrane fission. These results confirm the membrane remodeling activity of BDLP and suggest that IniA mediates TB drug-resistance through fission activity to maintain plasma membrane integrity.


    Organizational Affiliation

    University of Chinese Academy of Sciences, Beijing, 100101, China.,Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.,School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, 4072, QLD, Australia.,National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, 100101, China. huj@ibp.ac.cn.,Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China. lijun@sibcb.ac.cn.,State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, and Tianjin Key Laboratory of Protein Sciences, Tianjin, 300071, China.,State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, and Tianjin Key Laboratory of Protein Sciences, Tianjin, 300071, China. huj@ibp.ac.cn.,CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China. lijun@sibcb.ac.cn.,CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China.,National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, 100101, China.,Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China.




Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
Isoniazid inducible gene protein IniA
A, B
606Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)Mutation(s): 0 
Gene Names: iniA
Find proteins for I7FE16 (Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155))
Go to UniProtKB:  I7FE16
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.211 Å
  • R-Value Free: 0.258 
  • R-Value Work: 0.219 
  • Space Group: P 31
Unit Cell:
Length (Å)Angle (°)
a = 91.760α = 90.00
b = 91.760β = 90.00
c = 137.346γ = 120.00
Software Package:
Software NamePurpose
HKL-2000data scaling
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction
PHASERphasing

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Chinese Academy of SciencesChinaXDB08020200
Ministry of Science and Technology (China)China2016YFA0500201
Ministry of Science and Technology (China)China2017YFC0840300
Ministry of Science and Technology (China)China2014CB542800
Ministry of Science and Technology (China)China2014CBA02003
National Natural Science Foundation of ChinaChina813300237
National Natural Science Foundation of ChinaChina81520108019
National Natural Science Foundation of ChinaChina31630020
National Natural Science Foundation of ChinaChina31500607
Chinese Academy of SciencesChinaXDPB10

Revision History 

  • Version 1.0: 2019-09-11
    Type: Initial release