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

J 2005

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

MITCHELL, Edward, Charles SABIN, Lenka ŠNAJDROVÁ, Martina POKORNÁ, Stephanie PERRET et. al.

Basic information

Original name

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

Name in Czech

Vysoká afinita vazby fukosy u lektinu Pseudomonas aeruginosa lectin PA-IIL: krystalová struktura komplexu s vysokým rozlišením 1.0 A v kombinaci s termodynamickými metodami a přístupy výpočetní chemie

Authors

MITCHELL, Edward (250 France), Charles SABIN (250 France), Lenka ŠNAJDROVÁ (203 Czech Republic), Martina POKORNÁ (203 Czech Republic), Stephanie PERRET (250 France), Catherine GAUTIER (250 France), Ctirad HOFR (203 Czech Republic), Nechama GILBOA-GARBER (376 Israel), Jaroslav KOČA (203 Czech Republic), Michaela WIMMEROVÁ (203 Czech Republic, guarantor) and Anne IMBERTY (250 France)

Edition

Proteins: Structure, Function, and Bioinformatics, Wiley, 2005, 0887-3585

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 4.684

RIV identification code

RIV/00216224:14310/05:00013567

Organization unit

Faculty of Science

UT WoS

000226695900022

Keywords in English

lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure

Abstract

ORIG CZ

V originále

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.

In Czech

Links

LN00A016, research and development project

Name: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Center

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

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. Proteins: Structure, Function, and Bioinformatics. Wiley, 2005, vol. 58, No 3, p. 735-746. ISSN 0887-3585.

@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.

Detailed Information on Publication Record