4CC7

Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.97 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Details of Human Tuba Recruitment by Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading.

Polle, L.Rigano, L.A.Julian, R.Ireton, K.Schubert, W.

(2014) Structure 22: 304

  • DOI: https://doi.org/10.1016/j.str.2013.10.017
  • Primary Citation of Related Structures:  
    4CC2, 4CC3, 4CC4, 4CC7

  • PubMed Abstract: 

    The human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners.


  • Organizational Affiliation

    Department of Biotechnology, University of the Western Cape, Bellville 7535, Cape Town, South Africa; Division of Structural Biology, Helmholtz-Centre for Infection Research, Braunschweig 38124, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DYNAMIN-BINDING PROTEIN
A, C, E, G, I
A, C, E, G, I, K, M
67Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q6XZF7 (Homo sapiens)
Explore Q6XZF7 
Go to UniProtKB:  Q6XZF7
PHAROS:  Q6XZF7
GTEx:  ENSG00000107554 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6XZF7
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN
B, D, F, H, J
B, D, F, H, J, L, N
12Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O00401 (Homo sapiens)
Explore O00401 
Go to UniProtKB:  O00401
PHAROS:  O00401
GTEx:  ENSG00000106299 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO00401
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
GOL
Query on GOL

Download Ideal Coordinates CCD File 
AA [auth K],
FA [auth M],
O [auth A],
R [auth C]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
CA [auth K]
DA [auth K]
EA [auth K]
HA [auth M]
IA [auth M]
CA [auth K],
DA [auth K],
EA [auth K],
HA [auth M],
IA [auth M],
JA [auth M],
KA [auth M],
P [auth A],
Q [auth A],
S [auth C],
T [auth C],
U [auth C],
V [auth E],
W [auth E],
X [auth G],
Y [auth G],
Z [auth I]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
MG
Query on MG

Download Ideal Coordinates CCD File 
BA [auth K],
GA [auth M]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.97 Å
  • R-Value Free: 0.215 
  • R-Value Work: 0.176 
  • R-Value Observed: 0.178 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 88.57α = 90
b = 88.57β = 90
c = 69.73γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-10-30
    Type: Initial release
  • Version 1.1: 2014-01-22
    Changes: Database references
  • Version 1.2: 2014-02-19
    Changes: Database references
  • Version 1.3: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description