2DI4

Crystal structure of the FtsH protease domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.79 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.254 

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This is version 1.2 of the entry. See complete history


Literature

Structure of the Whole Cytosolic Region of ATP-Dependent Protease FtsH

Suno, R.Niwa, H.Tsuchiya, D.Zhang, X.Yoshida, M.Morikawa, K.

(2006) Mol Cell 22: 575-585

  • DOI: https://doi.org/10.1016/j.molcel.2006.04.020
  • Primary Citation of Related Structures:  
    2DHR, 2DI4, 4EIW

  • PubMed Abstract: 

    An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.


  • Organizational Affiliation

    Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226-8503, Japan.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cell division protein ftsH homolog
A, B
238Aquifex aeolicusMutation(s): 0 
EC: 3.4.24
UniProt
Find proteins for O67077 (Aquifex aeolicus (strain VF5))
Explore O67077 
Go to UniProtKB:  O67077
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO67077
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.79 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.251 
  • R-Value Observed: 0.254 
  • Space Group: P 63
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 116.8α = 90
b = 116.8β = 90
c = 63.5γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-06-27
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Derived calculations, Version format compliance