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PDBsum entry 4ljh
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Sugar binding protein
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PDB id
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4ljh
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PDB id:
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| Name: |
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Sugar binding protein
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Title:
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Crystal structure of pseudomonas aeruginosa lectin leca complexed with 1-methyl-3-indolyl-b-d-galactopyranoside at 1.45 a resolution
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Structure:
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Pa-i galactophilic lectin. Chain: a, b, c, d. Synonym: pa-il, galactose-binding lectin. Engineered: yes
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Source:
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Pseudomonas aeruginosa. Organism_taxid: 208964. Strain: atcc 15692 / pao1 / 1c / prs 101 / lmg 12228. Gene: leca, pa1l, pa2570. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.45Å
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R-factor:
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0.191
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R-free:
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0.211
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Authors:
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R.U.Kadam,A.Stocker,J.L.Reymond
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Key ref:
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R.U.Kadam
et al.
(2013).
CH-π "T-shape" interaction with histidine explains binding of aromatic galactosides to Pseudomonas aeruginosa lectin LecA.
Acs Chem Biol,
8,
1925-1930.
PubMed id:
DOI:
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Date:
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04-Jul-13
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Release date:
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30-Oct-13
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PROCHECK
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Headers
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References
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Q05097
(PA1L_PSEAE) -
PA-I galactophilic lectin from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Seq:
Struc:
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122 a.a.
121 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Acs Chem Biol
8:1925-1930
(2013)
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PubMed id:
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CH-π "T-shape" interaction with histidine explains binding of aromatic galactosides to Pseudomonas aeruginosa lectin LecA.
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R.U.Kadam,
D.Garg,
J.Schwartz,
R.Visini,
M.Sattler,
A.Stocker,
T.Darbre,
J.L.Reymond.
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ABSTRACT
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The galactose specific lectin LecA mediates biofilm formation in the
opportunistic pathogen P. aeruginosa . The interaction between LecA and aromatic
β-galactoside biofilm inhibitors involves an intermolecular CH-π T-shape
interaction between C(ε1)-H of residue His50 in LecA and the aromatic ring of
the galactoside aglycone. The generality of this interaction was tested in a
diverse family of β-galactosides. LecA binding to aromatic β-galactosides (KD
∼ 8 μM) was consistently stronger than to aliphatic β-galactosides (KD ∼
36 μM). The CH-π interaction was observed in the X-ray crystal structures of
six different LecA complexes, with shorter than the van der Waals distances
indicating productive binding. Related XH/cation/π-π interactions involving
other residues were identified in complexes of aromatic glycosides with a
variety of carbohydrate binding proteins such as concanavalin A. Exploiting such
interactions might be generally useful in drug design against these targets.
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