2CG4

Structure of E.coli AsnC


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.294 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Insight Into Gene Transcriptional Regulation and Effector Binding by the Lrp/Asnc Family.

Thaw, P.Sedelnikova, S.E.Muranova, T.Wiese, S.Ayora, S.Alonso, J.C.Brinkman, A.B.Akerboom, J.Van Der Oost, J.Rafferty, J.B.

(2006) Nucleic Acids Res 34: 1439

  • DOI: https://doi.org/10.1093/nar/gkl009
  • Primary Citation of Related Structures:  
    2CFX, 2CG4

  • PubMed Abstract: 

    The Lrp/AsnC family of transcriptional regulatory proteins is found in both archaea and bacteria. Members of the family influence cellular metabolism in both a global (Lrp) and specific (AsnC) manner, often in response to exogenous amino acid effectors. In the present study we have determined both the first bacterial and the highest resolution structures for members of the family. Escherichia coli AsnC is a specific gene regulator whose activity is triggered by asparagine binding. Bacillus subtilis LrpC is a global regulator involved in chromosome condensation. Our AsnC-asparagine structure is the first for a regulator-effector complex and is revealed as an octameric disc. Key ligand recognition residues are identified together with a route for ligand access. The LrpC structure reveals a stable octamer supportive of a topological role in dynamic DNA packaging. The structures yield significant clues to the functionality of Lrp/AsnC-type regulators with respect to ligand binding and oligomerization states as well as to their role in specific and global DNA regulation.


  • Organizational Affiliation

    Department of Molecular Biology and Biotechnology, Krebs Institute, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
REGULATORY PROTEIN ASNC
A, B
152Escherichia coliMutation(s): 1 
UniProt
Find proteins for P0ACI6 (Escherichia coli (strain K12))
Explore P0ACI6 
Go to UniProtKB:  P0ACI6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0ACI6
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.294 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.232 
  • Space Group: P 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 103.117α = 90
b = 103.117β = 90
c = 52.401γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-04
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-04-28
    Changes: Data collection, Derived calculations, Other