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@article{562341,
author = {Mitchell, Edward and Sabin, Charles and Šnajdrová, Lenka and Pokorná, Martina and Perret, Stephanie and Gautier, Catherine and Hofr, Ctirad and GilboaandGarber, Nechama and Koča, Jaroslav and Wimmerová, Michaela and Imberty, Anne},
article_number = {3},
keywords = {lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure},
language = {eng},
issn = {0887-3585},
journal = {Proteins: Structure, Function, and Bioinformatics},
title = {High affinity fucose binding of Pseudomonas aeruginosa lectin PA-IIL: 1.0 A resolution crystal structure of the complex combined with thermodynamics and computational chemistry approaches},
volume = {58},
year = {2005}
}
TY - JOUR
ID - 562341
AU - Mitchell, Edward - Sabin, Charles - Šnajdrová, Lenka - Pokorná, Martina - Perret, Stephanie - Gautier, Catherine - Hofr, Ctirad - Gilboa-Garber, Nechama - Koča, Jaroslav - Wimmerová, Michaela - Imberty, Anne
PY - 2005
TI - High affinity fucose binding of Pseudomonas aeruginosa lectin PA-IIL: 1.0 A resolution crystal structure of the complex combined with thermodynamics and computational chemistry approaches
JF - Proteins: Structure, Function, and Bioinformatics
VL - 58
IS - 3
SP - 735-746
EP - 735-746
PB - Wiley
SN - 08873585
KW - lectin
KW - Pseudomonas aeruginosa
KW - cystic fibrosis
KW - crystal structure
N2 - PA-IIL is a fucose-binding lectin from Pseudomonas aeruginosa that is closely related to the virulence factors of the bacterium. Previous structural studies have revealed a new carbohydrate-binding mode with direct involvement of two calcium ions (Mitchell E, Houles C, Sudakevitz D, Wimmerova M, Gautier C, Perez S,Wu AM, Gilboa-Garber N Imberty A. Structural basis for selective recognition of oligosaccharides from cystic fibrosis patients by the lectin PA-IIL of Pseudomonas aeruginosa. Nat Struct Biol 2002;9:918921). A combination of thermodynamic, structural, and computational methods has been used to study the basis of the high affinity for the monosaccharide ligand. A titration microcalorimetry study indicated that the high affinity is enthalpy driven. The crystal structure of the tetrameric PA-IIL in complex with fucose and calcium was refined to 1.0 Ĺ resolution and, in combination with modeling, allowed a proposal to be made for the hydrogen-bond network in the binding site. Calculations of partial charges using ab initio computational chemistry methods indicated that extensive delocalization of charges between the calcium ions, the side chains of the protein- binding site and the carbohydrate ligand is responsible for the high enthalpy of binding and therefore for the unusually high affinity observed for this unique mode of carbohydrate recognition.
ER -
MITCHELL, Edward, Charles SABIN, Lenka ŠNAJDROVÁ, Martina POKORNÁ, Stephanie PERRET, Catherine GAUTIER, Ctirad HOFR, Nechama GILBOA-GARBER, Jaroslav KOČA, Michaela WIMMEROVÁ and Anne IMBERTY. High affinity fucose binding of Pseudomonas aeruginosa lectin PA-IIL: 1.0 A resolution crystal structure of the complex combined with thermodynamics and computational chemistry approaches. \textit{Proteins: Structure, Function, and Bioinformatics}. Wiley, 2005, vol.~58, No~3, p.~735-746. ISSN~0887-3585.
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