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PDBsum entry 5d2a

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protein ligands metals Protein-protein interface(s) links
Sugar binding protein PDB id
5d2a

 

 

 

 

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Contents
Protein chains
114 a.a.
Ligands
ALA-PRO-ALA-LYS-
PHE-CYS
ALA-PRO-ALA ×2
PHB-GAL
ZDC ×2
Metals
_CA ×4
Waters ×79
PDB id:
5d2a
Name: Sugar binding protein
Title: Bifunctional dendrimers
Structure: Fucose-binding lectin. Chain: a, b. Synonym: fucose-binding lectin pa-iil,photopexin a,pseudomonas aeruginosa genome assembly pae221. Engineered: yes. Zdc-ala-pro-ala-lys-phe-cys-ala-pro-ala-phb-gal. Chain: c. Engineered: yes. Zdc-ala-pro-ala-lys-phe-cys-ala-pro-ala-phb-gal.
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: lecb, ers445055_01627, pa8380_17510, pae221_03716, pamh19_1713, yq19_10010. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630.
Resolution:
2.13Å     R-factor:   0.209     R-free:   0.246
Authors: G.Michaud,R.Visini,A.Stocker,T.Darbre,J.L.Reymond
Key ref: G.Michaud et al. (2016). Overcoming antibiotic resistance in Pseudomonas aeruginosa biofilms using glycopeptide dendrimers. Chem Sci, 7, 166-182. PubMed id: 29896342
Date:
05-Aug-15     Release date:   10-Feb-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9HYN5  (Q9HYN5_PSEAE) -  Fucose-binding lectin PA-IIL from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc:
115 a.a.
114 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Chem Sci 7:166-182 (2016)
PubMed id: 29896342  
 
 
Overcoming antibiotic resistance in Pseudomonas aeruginosa biofilms using glycopeptide dendrimers.
G.Michaud, R.Visini, M.Bergmann, G.Salerno, R.Bosco, E.Gillon, B.Richichi, C.Nativi, A.Imberty, A.Stocker, T.Darbre, J.L.Reymond.
 
  ABSTRACT  
 
Antibiotic resistance in the opportunistic pathogen Pseudomonas aeruginosa is partly caused by biofilms forming a physical barrier to antibiotic penetration. Here we focused on modifying tetravalent glycopeptide dendrimer ligands of P. aeruginosa lectins LecB or LecA to increase their biofilm inhibition activity. First heteroglycoclusters were investigated displaying one pair each of LecB specific fucosyl groups and LecA specific galactosyl groups and binding simultaneously to both lectins, one of which gave the first fully resolved crystal structure of a peptide dendrimer as LecB complex providing a structural model for dendrimer-lectin interactions (PDB ; 5D2A). Biofilm inhibition was increased by introducing additional cationic residues in these dendrimers but resulted in bactericidal effects similar to those of non-glycosylated polycationic antimicrobial peptide dendrimers. In a second approach dendrimers displaying four copies of the natural LecB ligand Lewisa were prepared leading to slightly stronger LecB binding and biofilm inhibition. Finally synergistic application of a LecB specific non-bactericidal antibiofilm dendrimer with the antibiotic tobramycin at sub-inhibitory concentrations of both compounds allowed effective biofilm inhibition and dispersal.
 

 

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