4KWE

GDP-bound, double-stranded, curved FtsZ protofilament structure

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.91 Å
  • R-Value Free: 0.267 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.242 

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This is version 1.2 of the entry. See complete history. 


Literature

FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation

Li, Y., Hsin, J., Zhao, L., Cheng, Y., Shang, W., Huang, K.C., Wang, H.W., Ye, S.

(2013) Science 341: 392-395

  • DOI: https://doi.org/10.1126/science.1239248
  • Primary Citation of Related Structures:  
    4KWE

  • PubMed Abstract: 

    The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a structure at the division site termed the "Z ring". During cytokinesis, the Z ring exerts a constrictive force on the membrane by using the chemical energy of guanosine triphosphate hydrolysis. However, the structural basis of this constriction remains unresolved. Here, we present the crystal structure of a guanosine diphosphate-bound Mycobacterium tuberculosis FtsZ protofilament, which exhibits a curved conformational state. The structure reveals a longitudinal interface that is important for function. The protofilament curvature highlights a hydrolysis-dependent conformational switch at the T3 loop that leads to longitudinal bending between subunits, which could generate sufficient force to drive cytokinesis.

    • Organizational Affiliation: 

    Life Sciences Institute, Zhejiang University, Hangzhou, 310058 Zhejiang, P.R. China.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division protein FtsZ
A, B, C
382Mycobacterium tuberculosisMutation(s): 0 
Gene Names: ftsZ, MT2209, MTCY270.18, Rv2150c
UniProt
Find proteins for P9WN95 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WN95 
Go to UniProtKB:  P9WN95
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WN95
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.91 Å
  • R-Value Free: 0.267 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.242 
  • Space Group: P 64 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 132.509α = 90
b = 132.509β = 90
c = 321.549γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASESphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-07-31
    Type: Initial release
  • Version 1.1: 2013-09-04
    Changes: Database references
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references, Derived calculations, Refinement description