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.

Základní údaje

Originální název

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

Název česky

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

Autoři

MITCHELL, Edward (250 Francie), Charles SABIN (250 Francie), Lenka ŠNAJDROVÁ (203 Česká republika), Martina POKORNÁ (203 Česká republika), Stephanie PERRET (250 Francie), Catherine GAUTIER (250 Francie), Ctirad HOFR (203 Česká republika), Nechama GILBOA-GARBER (376 Izrael), Jaroslav KOČA (203 Česká republika), Michaela WIMMEROVÁ (203 Česká republika, garant) a Anne IMBERTY (250 Francie)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 4.684

Kód RIV

RIV/00216224:14310/05:00013567

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000226695900022

Klíčová slova anglicky

lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure

Štítky

Crystal Structure, cystic fibrosis, lectin, Pseudomonas aeruginosa

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 1. 2007 15:32, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

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.

Česky

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

MITCHELL, Edward, Charles SABIN, Lenka ŠNAJDROVÁ, Martina POKORNÁ, Stephanie PERRET, Catherine GAUTIER, Ctirad HOFR, Nechama GILBOA-GARBER, Jaroslav KOČA, Michaela WIMMEROVÁ a 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, roč. 58, č. 3, s. 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 a 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, roč.~58, č.~3, s.~735-746. ISSN~0887-3585.

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