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.

Basic information

Original name

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

Authors

WIMMEROVÁ, Michaela (203 Czech Republic, guarantor), Edward MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Jean-Frederick SANCHEZ (250 France), Catherine GAUTIER (250 France) and Anne IMBERTY (250 France)

Edition

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

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: 6.482

RIV identification code

RIV/00216224:14310/03:00008832

Organization unit

Faculty of Science

Keywords in English

aleuria aurantia; lectin; crystal structure

Abstract

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.

Links

LN00A016, research and development project

Name: BIOMOLEKULÁRNÍ CENTRUM

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

Citovat

WIMMEROVÁ, Michaela, Edward MITCHELL, Jean-Frederick SANCHEZ, Catherine GAUTIER and 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, vol. 278, No 29, p. 27059-27067, 8 pp. 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 and 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, vol.~278, No~29, p.~27059-27067, 8 pp. ISSN~0021-9258.

Detailed Information on Publication Record