Aleuria aurantia lectin displays novel binding mode for fucose.
Crystal structure and ligand interaction of a new family of
fucolectins.

D 2003

Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.

WIMMEROVÁ, Michaela, Edward MITCHELL, Jean-Frederic SANCHEZ, Catherine GAUTIER, Hugues LORTAT-JACOB et. al.

Basic information

Original name

Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.

Authors

WIMMEROVÁ, Michaela (203 Czech Republic, guarantor), Edward MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Jean-Frederic SANCHEZ (250 France), Catherine GAUTIER (250 France), Hugues LORTAT-JACOB (250 France), Nechama GILBOA-GARBER (376 Israel) and Anne IMBERTY (250 France)

Edition

Grenoble, France, 12th European Carbohydrate Symposium, p. 93-93, 2003

Publisher

CERMAV-CNRS

Other information

Language

English

Type of outcome

Stať ve sborníku

Field of Study

10600 1.6 Biological sciences

Country of publisher

France

Confidentiality degree

není předmětem státního či obchodního tajemství

RIV identification code

RIV/00216224:14310/03:00008864

Organization unit

Faculty of Science

Keywords in English

aleuria aurantia; lectin; crystal structure; fungi

Abstract

V originále

Aleuria aurantia lectin (AAL) is a fungal protein that specifically recognised fucose moiety in glycans. The crystal structure of AAL complexed with fucose has been solved at 1.5 A resolution. AAL displays a dimer composition, each subunit consists of a six-bladed beta-propeller fold and of a small antiparallel two-strands beta-sheet that play a role in dimerization. Primary sequence of AAL contains six internal repeats [1] corresponded to particular blades, crystal structure reveals five fucose molecules per AAL monomer in binding sites formed by two adjacent blades. Surface plasmon resonance experiments have been performed on a series of fucose containing oligosaccharides to determine equilibrium dissociation constants for lectine-oligosaccharide interaction. Measurements confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. AAL shows high sequence similarity with a lectin from plant pathogenic bacterium Ralstonia solanacearum (RSL) [2]. As RSL is smaller (91 amino acid residues compared to 312 of AAL), only two typical internal repeats can be found in sequence. SPR studies demonstrated that RSL shares similar specificity as AAL but highly prefers alpha-Fuc1-2 linkage. [1] Fukumori, F., Takeuchi, N., Hagiwara, T., Ohbayashi, H., Endo, T., Kochibe, N., Nagata, Y., and Kobata, A J. Biochem. 107, 190-196 (1990) [2] Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., J. Biochem. 132, 353-358 (2002)

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-Frederic SANCHEZ, Catherine GAUTIER, Hugues LORTAT-JACOB, Nechama GILBOA-GARBER and Anne IMBERTY. Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins. In 12th European Carbohydrate Symposium. Grenoble, France: CERMAV-CNRS, 2003, p. 93.

@inproceedings{488300,
   author = {Wimmerová, Michaela and Mitchell, Edward and Sanchez, JeanandFrederic and Gautier, Catherine and LortatandJacob, Hugues and GilboaandGarber, Nechama and Imberty, Anne},
   address = {Grenoble, France},
   booktitle = {12th European Carbohydrate Symposium},
   keywords = {aleuria aurantia; lectin; crystal structure; fungi},
   language = {eng},
   location = {Grenoble, France},
   pages = {93-93},
   publisher = {CERMAV-CNRS},
   title = {Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.},
   year = {2003}
}

TY  - JOUR
ID  - 488300
AU  - Wimmerová, Michaela - Mitchell, Edward - Sanchez, Jean-Frederic - Gautier, Catherine - Lortat-Jacob, Hugues - Gilboa-Garber, Nechama - Imberty, Anne
PY  - 2003
TI  - Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins.
PB  - CERMAV-CNRS
CY  - Grenoble, France
KW  - aleuria aurantia
KW  - lectin
KW  - crystal structure
KW  - fungi
N2  - Aleuria aurantia lectin (AAL) is a fungal protein that specifically recognised fucose moiety in glycans. The crystal structure of AAL complexed with fucose has been solved at 1.5 A resolution. AAL displays a dimer composition, each subunit consists of a six-bladed beta-propeller fold and of a small antiparallel two-strands beta-sheet that play a role in dimerization. Primary sequence of AAL contains six internal repeats [1] corresponded to particular blades, crystal structure reveals five fucose molecules per AAL monomer in binding sites formed by two adjacent blades. Surface plasmon resonance experiments have been performed on a series of fucose containing oligosaccharides to determine equilibrium dissociation constants for lectine-oligosaccharide interaction. Measurements confirm the broad specificity of the lectin, with a slight preference for alpha-Fuc1-2Gal disaccharide. AAL shows high sequence similarity with a lectin from plant pathogenic bacterium Ralstonia solanacearum (RSL) [2]. As RSL is smaller (91 amino acid residues compared to 312 of AAL), only two typical internal repeats can be found in sequence. SPR studies demonstrated that RSL shares similar specificity as AAL but highly prefers alpha-Fuc1-2 linkage. [1] Fukumori, F., Takeuchi, N., Hagiwara, T., Ohbayashi, H., Endo, T., Kochibe, N., Nagata, Y., and Kobata, A J. Biochem. 107, 190-196 (1990) [2] Sudakevitz, D., Imberty, A., and Gilboa-Garber, N., J. Biochem. 132, 353-358 (2002)
ER  -

WIMMEROVÁ, Michaela, Edward MITCHELL, Jean-Frederic SANCHEZ, Catherine GAUTIER, Hugues LORTAT-JACOB, Nechama GILBOA-GARBER and Anne IMBERTY. Aleuria aurantia lectin displays novel binding mode for fucose. Crystal structure and ligand interaction of a new family of fucolectins. In \textit{12th European Carbohydrate Symposium}. Grenoble, France: CERMAV-CNRS, 2003, p.~93.

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