3KZ3

A structure of a lambda repressor fragment mutant


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Work: 0.188 
  • R-Value Observed: 0.189 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A survey of lambda repressor fragments from two-state to downhill folding.

Liu, F.Gao, Y.G.Gruebele, M.

(2010) J Mol Biol 397: 789-798

  • DOI: https://doi.org/10.1016/j.jmb.2010.01.071
  • Primary Citation of Related Structures:  
    3KZ3

  • PubMed Abstract: 

    We survey the two-state to downhill folding transition by examining 20 lambda(6-85)* mutants that cover a wide range of stabilities and folding rates. We investigated four new lambda(6-85)* mutants designed to fold especially rapidly. Two were engineered using the core remodeling of Lim and Sauer, and two were engineered using Ferreiro et al.'s frustratometer. These proteins have probe-dependent melting temperatures as high as 80 degrees C and exhibit a fast molecular phase with the characteristic temperature dependence of the amplitude expected for downhill folding. The survey reveals a correlation between melting temperature and downhill folding previously observed for the beta-sheet protein WW domain. A simple model explains this correlation and predicts the melting temperature at which downhill folding becomes possible. An X-ray crystal structure with a 1.64-A resolution of a fast-folding mutant fragment shows regions of enhanced rigidity compared to the full wild-type protein.


  • Organizational Affiliation

    Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Repressor protein CI
A, B
80Lambdavirus lambdaMutation(s): 4 
Gene Names: CI
UniProt
Find proteins for P03034 (Escherichia phage lambda)
Explore P03034 
Go to UniProtKB:  P03034
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03034
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.64 Å
  • R-Value Work: 0.188 
  • R-Value Observed: 0.189 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 32.63α = 90
b = 58.71β = 98.18
c = 42.85γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
AMoREphasing
SHELXL-97refinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2021-10-13
    Changes: Database references
  • Version 1.3: 2024-02-21
    Changes: Data collection