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Cell adhesion PDB id
2ver
Jmol
Contents
Protein chains
143 a.a. *
110 a.a. *
Ligands
MTN ×3
* Residue conservation analysis
PDB id:
2ver
Name: Cell adhesion
Title: Structural model for the complex between the dr adhesins and carcinoembryonic antigen (cea)
Structure: Afimbrial adhesin afa-iii. Chain: a. Fragment: residues 38-160. Synonym: afae. Engineered: yes. Arcinoembryonic antigen-related cell adhesion mol chain: n. Fragment: n domain, residues 35-144. Synonym: cea, carcinoembryonic antigen, meconium antigen 10
Source: Escherichia coli. Organism_taxid: 562. Strain: dr/afa. Expressed in: escherichia coli. Expression_system_taxid: 511693. Homo sapiens. Human. Organism_taxid: 9606.
NMR struc: 1 models
Authors: N.Korotkova,Y.Yang,I.Le Trong,E.Cota,B.Demeler,J.Marchant,W. R.E.Stenkamp,S.L.Moseley,S.Matthews
Key ref: N.Korotkova et al. (2008). Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Mol Microbiol, 67, 420-434. PubMed id: 18086185 DOI: 10.1111/j.1365-2958.2007.06054.x
Date:
26-Oct-07     Release date:   08-Jan-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q57254  (AFAE3_ECOLX) -  Afimbrial adhesin AFA-III
Seq:
Struc: 		160 a.a.
143 a.a.
Protein chain
Pfam   ArchSchema ?
P06731  (CEAM5_HUMAN) -  Carcinoembryonic antigen-related cell adhesion molecule 5
Seq:
Struc: 		 
Seq:
Struc: 		702 a.a.
110 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
DOI no: 10.1111/j.1365-2958.2007.06054.x Mol Microbiol 67:420-434 (2008)
PubMed id: 18086185  
 
 
Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation.
N.Korotkova, Y.Yang, I.Le Trong, E.Cota, B.Demeler, J.Marchant, W.E.Thomas, R.E.Stenkamp, S.L.Moseley, S.Matthews.
 
  ABSTRACT  
 
Carcinoembryonic antigen (CEA)-related cell adhesion molecules (CEACAMs) are host receptors for the Dr family of adhesins of Escherichia coli. To define the mechanism for binding of Dr adhesins to CEACAM receptors, we carried out structural studies on the N-terminal domain of CEA and its complex with the Dr adhesin. The crystal structure of CEA reveals a dimer similar to other dimers formed by receptors with IgV-like domains. The structure of the CEA/Dr adhesin complex is proposed based on NMR spectroscopy and mutagenesis data in combination with biochemical characterization. The Dr adhesin/CEA interface overlaps appreciably with the region responsible for CEA dimerization. Binding kinetics, mutational analysis and spectroscopic examination of CEA dimers suggest that Dr adhesins can dissociate CEA dimers prior to the binding of monomeric forms. Our conclusions include a plausible mechanism for how E. coli, and perhaps other bacterial and viral pathogens, exploit CEACAMs. The present structure of the complex provides a powerful tool for the design of novel inhibitory strategies to treat E. coli infections.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21458574 H.Czepczyńska-Krężel, M.Czerwinski, A.Krężel, and A.Krop-Watorek (2011).
Isolation of carcinoembryonic antigen N-terminal domains (N-A1) from soluble aggregates.
  Protein Expr Purif, 78, 78-85.  
21352462 V.Liévin-Le Moal, I.Beau, C.Rougeaux, I.Kansau, S.Fabrega, C.Brice, N.Korotkova, S.L.Moseley, and A.L.Servin (2011).
Apical expression of human full-length hCEACAM1-4L protein renders the Madin Darby Canine Kidney cells responsive to lipopolysaccharide leading to TLR4-dependent Erk1/2 and p38 MAPK signalling.
  Cell Microbiol, 13, 764-785.  
20349311 B.Zalewska-Piatek, M.Kur, S.Wilkanowicz, R.Piatek, and J.Kur (2010).
The DraC usher in Dr fimbriae biogenesis of uropathogenic E. coli Dr(+) strains.
  Arch Microbiol, 192, 351-363.  
19966814 M.A.Croxen, and B.B.Finlay (2010).
Molecular mechanisms of Escherichia coli pathogenicity.
  Nat Rev Microbiol, 8, 26-38.  
20017116 R.L.Rich, and D.G.Myszka (2010).
Grading the commercial optical biosensor literature-Class of 2008: 'The Mighty Binders'.
  J Mol Recognit, 23, 1.  
19948502 E.Klaile, O.Vorontsova, K.Sigmundsson, M.M.Müller, B.B.Singer, L.G.Ofverstedt, S.Svensson, U.Skoglund, and B.Obrink (2009).
The CEACAM1 N-terminal Ig domain mediates cis- and trans-binding and is essential for allosteric rearrangements of CEACAM1 microclusters.
  J Cell Biol, 187, 553-567.  
18992408 A.M.Lowe, C.P.Yansouni, and M.A.Behr (2008).
Causality and gastrointestinal infections: Koch, Hill, and Crohn's.
  Lancet Infect Dis, 8, 720-726.  
18559426 N.Korotkova, Y.Yarova-Yarovaya, V.Tchesnokova, N.Yazvenko, M.A.Carl, A.E.Stapleton, and S.L.Moseley (2008).
Escherichia coli DraE adhesin-associated bacterial internalization by epithelial cells is promoted independently by decay-accelerating factor and carcinoembryonic antigen-related cell adhesion molecule binding and does not require the DraD invasin.
  Infect Immun, 76, 3869-3880.  
18497748 R.Conners, D.J.Hill, E.Borodina, C.Agnew, S.J.Daniell, N.M.Burton, R.B.Sessions, A.R.Clarke, L.E.Catto, D.Lammie, T.Wess, R.L.Brady, and M.Virji (2008).
The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil.
  EMBO J, 27, 1779-1789.
PDB code: 2qih
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.