2ANE

Crystal structure of N-terminal domain of E.Coli Lon Protease


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Crystal structure of the N-terminal domain of E. coli Lon protease.

Li, M.Rasulova, F.Melnikov, E.E.Rotanova, T.V.Gustchina, A.Maurizi, M.R.Wlodawer, A.

(2005) Protein Sci 14: 2895-2900

  • DOI: https://doi.org/10.1110/ps.051736805
  • Primary Citation of Related Structures:  
    2ANE

  • PubMed Abstract: 

    We report here the first crystal structure of the N-terminal domain of an A-type Lon protease. Lon proteases are ubiquitous, multidomain, ATP-dependent enzymes with both highly specific and non-specific protein binding, unfolding, and degrading activities. We expressed and purified a stable, monomeric 119-amino acid N-terminal subdomain of the Escherichia coli A-type Lon protease and determined its crystal structure at 2.03 A (Protein Data Bank [PDB] code 2ANE). The structure was solved in two crystal forms, yielding 14 independent views. The domain exhibits a unique fold consisting primarily of three twisted beta-sheets and a single long alpha-helix. Analysis of recent PDB depositions identified a similar fold in BPP1347 (PDB code 1ZBO), a 203-amino acid protein of unknown function from Bordetella parapertussis, crystallized as part of a structural genomics effort. BPP1347 shares sequence homology with Lon N-domains and with a family of other independently expressed proteins of unknown functions. We postulate that, as is the case in Lon proteases, this structural domain represents a general protein and polypeptide interaction domain.


  • Organizational Affiliation

    Macromolecular Crystallography Laboratory, National Cancer Institute, Building 536, Room 5, Frederick, MD 21702-1201, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent protease La
A, B, C, D, E
A, B, C, D, E, F, G, H
125Escherichia coliMutation(s): 0 
Gene Names: loncapRdeglopAmuc
EC: 3.4.21.53
UniProt
Find proteins for P0A9M0 (Escherichia coli (strain K12))
Explore P0A9M0 
Go to UniProtKB:  P0A9M0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A9M0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.03 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.212 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 90.61α = 90
b = 53.445β = 107.5
c = 111.973γ = 90
Software Package:
Software NamePurpose
MAR345data collection
SCALEPACKdata scaling
EPMRphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-11-01
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references