Six-bladed ß -propeller fold and novel fucose recognition mode
for Aleuria aurantia lectin

J 2003

Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin

WIMMEROVÁ, Michaela; Edward MITCHELL; Jean-Frederick SANCHEZ; Catherine GAUTIER; Anne IMBERTY et. al.

Základní údaje

Originální název

Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin

Autoři

WIMMEROVÁ, Michaela; Edward MITCHELL; Jean-Frederick SANCHEZ; Catherine GAUTIER a Anne IMBERTY

Vydání

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2003, 0021-9258

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: 6.482

Kód RIV

RIV/00216224:14310/03:00008832

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

aleuria aurantia; lectin; crystal structure

Štítky

aleuria aurantia, Crystal Structure, lectin

Příznaky

Mezinárodní význam, Recenzováno

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

Anotace

V originále

Aleuria aurantia lectin is a fungal protein composed of two identical 312-amino acid subunits that specifically recognizes fucosylated glycans. The crystal structure of the lectin complexed with fucose reveals that each monomer consists of a six-bladed beta-propeller fold and of a small antiparallel two-stranded beta-sheet that plays a role in dimerization. Five fucose residues were located in binding pockets between the adjacent propeller blades. Due to repeats in the amino acid sequence, there are strong similarities between the sites. Oxygen atoms O-3, O-4, and O-5 of fucose are involved in hydrogen bonds with side chains of amino acids conserved in all repeats, whereas O-1 and O-2 interact with a large number of water molecules. The nonpolar face of each fucose residue is stacked against the aromatic ring of a Trp or Tyr amino acid, and the methyl group is located in a highly hydrophobic pocket. Depending on the precise binding site geometry, the alpha-or beta-anomer of the fucose ligand is observed bound in the crystal. Surface plasmon resonance experiments conducted on a series of oligosaccharides confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. This multivalent carbohydrate recognition fold is a new prototype of lectins that is proposed to be involved in the host recognition strategy of several pathogenic organisms including not only the fungi Aspergillus but also the phytopathogenic bacterium Ralstonia solanacearum.

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

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

Citovat

WIMMEROVÁ, Michaela; Edward MITCHELL; Jean-Frederick SANCHEZ; Catherine GAUTIER a Anne IMBERTY. Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2003, roč. 278, č. 29, s. 27059-27067, 8 s. ISSN 0021-9258.

@article{488052,
   author = {Wimmerová, Michaela and Mitchell, Edward and Sanchez, JeanandFrederick and Gautier, Catherine and Imberty, Anne},
   article_location = {Bethesda, USA},
   article_number = {29},
   keywords = {aleuria aurantia; lectin; crystal structure},
   language = {eng},
   issn = {0021-9258},
   journal = {Journal of Biological Chemistry},
   title = {Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin},
   volume = {278},
   year = {2003}
}

TY  - JOUR
ID  - 488052
AU  - Wimmerová, Michaela - Mitchell, Edward - Sanchez, Jean-Frederick - Gautier, Catherine - Imberty, Anne
PY  - 2003
TI  - Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin
JF  - Journal of Biological Chemistry
VL  - 278
IS  - 29
SP  - 27059-27067
EP  - 27059-27067
PB  - Amer. Soc. Biochem. Mol. Biol.
SN  - 00219258
KW  - aleuria aurantia
KW  - lectin
KW  - crystal structure
N2  - Aleuria aurantia lectin is a fungal protein composed of two identical 312-amino acid subunits that specifically recognizes fucosylated glycans. The crystal structure of the lectin complexed with fucose reveals that each monomer consists of a six-bladed beta-propeller fold and of a small antiparallel two-stranded beta-sheet that plays a role in dimerization. Five fucose residues were located in binding pockets between the adjacent propeller blades. Due to repeats in the amino acid sequence, there are strong similarities between the sites. Oxygen atoms O-3, O-4, and O-5 of fucose are involved in hydrogen bonds with side chains of amino acids conserved in all repeats, whereas O-1 and O-2 interact with a large number of water molecules. The nonpolar face of each fucose residue is stacked against the aromatic ring of a Trp or Tyr amino acid, and the methyl group is located in a highly hydrophobic pocket. Depending on the precise binding site geometry, the alpha-or beta-anomer of the fucose ligand is observed bound in the crystal. Surface plasmon resonance experiments conducted on a series of oligosaccharides confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. This multivalent carbohydrate recognition fold is a new prototype of lectins that is proposed to be involved in the host recognition strategy of several pathogenic organisms including not only the fungi Aspergillus but also the phytopathogenic bacterium Ralstonia solanacearum.
ER  -

WIMMEROVÁ, Michaela; Edward MITCHELL; Jean-Frederick SANCHEZ; Catherine GAUTIER a Anne IMBERTY. Six-bladed ß -propeller fold and novel fucose recognition mode for Aleuria aurantia lectin. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2003, roč.~278, č.~29, s.~27059-27067, 8 s. ISSN~0021-9258.

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