4CIL

YopM-InlB: Hybrid leucine-rich repeat protein

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 

wwPDB Validation   3D Report Full Report


This is version 1.6 of the entry. See complete history. 


Literature

Crystal Structure of an Engineered Yopm-Inlb Hybrid Protein.

Breitsprecher, D., Gherardi, E., Bleymuller, W.M., Niemann, H.H.

(2014) BMC Struct Biol 14: 12

  • DOI: https://doi.org/10.1186/1472-6807-14-12
  • Primary Citation of Related Structures:  
    4CIL

  • PubMed Abstract: 

    The multi-domain protein InlB (internalin B) from Listeria monocytogenes is an agonist of the human receptor tyrosine kinase MET. Only the internalin domain directly interacts with MET. The internalin domain consists of seven central leucine-rich repeats (LRRs) flanked by an N-terminal helical cap domain and a C-terminal immunoglobulin-like structure. A potential function of the N-terminal cap in receptor binding could so far not be demonstrated by deleting the cap, since the cap is also implicated in nucleating folding of the LRR domain.

    • Organizational Affiliation: 

    Department of Molecular Structural Biology, Helmholtz Centre for Infection Research, 38124 Braunschweig, Germany. Hartmut.Niemann@uni-bielefeld.de.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
YOPM-CAP, INTERNALIN B287Yersinia enterocolitica, Listeria monocytogenes EGD-e
This entity is chimeric		Mutation(s): 0 
UniProt
Find proteins for P0DQD2 (Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e))
Explore P0DQD2 
Go to UniProtKB:  P0DQD2
Find proteins for P74988 (Yersinia enterocolitica W22703)
Explore P74988 
Go to UniProtKB:  P74988
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP74988P0DQD2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.219 
  • R-Value Work: 0.175 
  • R-Value Observed: 0.177 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.21α = 90
b = 30.68β = 90.98
c = 135.39γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-04-02
    Type: Initial release
  • Version 1.1: 2014-04-09
    Changes: Database references
  • Version 1.2: 2017-03-15
    Changes: Source and taxonomy
  • Version 1.3: 2019-03-06
    Changes: Data collection, Experimental preparation
  • Version 1.4: 2019-05-08
    Changes: Data collection, Experimental preparation
  • Version 1.5: 2019-07-24
    Changes: Data collection
  • Version 1.6: 2023-12-20
    Changes: Data collection, Database references, Other, Refinement description