X-ray crystallographic characterization and phasing of a fucose-specific lectin from<i>Aleuria aurantia</i>

Fujihashi, M.; Peapus, Diane H.; Nakajima, Eijiro; Yamada, Tsuyoshi; Saito, Jun; Kita, Akiko; Higuchi, Yoshiki; Sugawara, Yoko; Andõ, Akira; Kamiya, Nobuo; Nagata, Yoshiho; Miki, Kunio

doi:10.1107/s0907444902022175

Cited by 11 publications

(11 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ligand position was not affected by the Trp conformation when compared to previously published AAL/Fuc structure. [ 1 , 38 ] To our knowledge, this phenomenon has never been reported previously for any known lectin–sugar or, in general, protein–carbohydrate complex.…”

Section: Discussionsupporting

confidence: 50%

“…The protein adopts the 6-bladed β-propeller fold ( Fig 2F ) highly similar to a previously determined structure of the AAL/Fuc complex. [ 1 ] No significant variations of the backbone conformation were observed between the chains of the AAL N224Q complex and previously determined structures,[ 1 , 38 ] with RMSD varying from 0.186 to 0.249 Å. Comparison of the AAL structures shows that all binding sites are rigid and do not change the structure upon the binding and so do not suggest possible cooperativity between the binding sites.…”

Section: Resultsmentioning

confidence: 70%

See 1 more Smart Citation

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

et al. 2017

View full text Add to dashboard Cite

Protein–carbohydrate interactions are very often mediated by the stacking CH–π interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate like ligands in 5 208 Trp containing motives. An appropriate model system to study such an interaction is the AAL lectin family where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with α-methyl-l-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp–carbohydrate complexes, which would suggest no substantial preference for one conformation over another.

show abstract

Section: Discussionsupporting

confidence: 50%

Section: Resultsmentioning

confidence: 70%

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

et al. 2017

View full text Add to dashboard Cite

show abstract

“…Additionally, crystal structure analysis of AAL [18,19] has shown that the 2 and 4 binding sites have glutamine (Q) residues in their fucose binding pockets that coordinate with other amino acids within the pocket to maintain a secondary structure required for high affinity fucose binding. In binding sites 3 and 5, an asparagine (N) is found in this position.…”

Section: Resultsmentioning

confidence: 99%

“…The Aleuria aurantia lectin (AAL) detects various fucose linkages (α-1,2; α-1,3; α-1,4; α-1,6) attached to either a N -acetylglucosamine (GlcNAc) or a galactose residue. The crystal structure for AAL has been solved by several groups and reveals that AAL monomers display a six-bladed β-propeller fold with five conserved fucose binding sites located between each blade [17-19]. The sixth site does not contain the conserved amino acids residues required to form the fucose binding pocket and it is proposed that the sixth site forms closure contacts between blades 1 and 6 to help stabilize the overall β-propeller structure [18].…”

Section: Introductionmentioning

confidence: 99%

Development of recombinant Aleuria aurantia lectins with altered binding specificities to fucosylated glycans

Romano

Mackay

Vong

et al. 2011

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Changes in glycosylation have long been associated with disease. While there are many methods to detect changes in glycosylation, plant derived lectins are often used to determine changes on specific proteins or molecules of interest. One change in glycosylation that has been observed by us and by others is a disease or antigen associated increase in fucosylation on N-linked glycans. To measure this change, the fucose binding Aleuria aurantia lectin (AAL) is often utilized in plate and solution based assays. AAL is a mushroom derived lectin that contains five fucose binding sites that preferentially bind fucose linked (α-1,3, α-1,2, α-,4, and α-1,6) to N-acetyllactosamine related structures. Recently, several reports by us and by others have indicated that specific fucose linkages found on certain serum biomarker glycoprotein's are more associated with disease than others. Taking a site-directed mutagenesis approach, we have created a set of recombinant AAL proteins that display altered binding affinities to different analytes containing various fucose linkages.

show abstract

“…However, there is only limited information about them, and although several crystals have been obtained, including the lectins from Flammulina veltipes (9), Pleurotus cornicopiae (10), Pleurotus ostreatus (11), Sclerotium rosfii (12), and Aleuria aurantia (13,14), no crystal structure has yet been determined.…”

mentioning

confidence: 99%

Crystal Structure of Fungal Lectin

Wimmerová

Mitchell

Sanchez

et al. 2003

Journal of Biological Chemistry

167

102

View full text Add to dashboard Cite

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 ␤-propeller fold and of a small antiparallel two-stranded ␤-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 ␣-or ␤-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 ␣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.

show abstract

X-ray crystallographic characterization and phasing of a fucose-specific lectin fromAleuria aurantia

Cited by 11 publications

References 17 publications

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL

Development of recombinant Aleuria aurantia lectins with altered binding specificities to fucosylated glycans

Crystal Structure of Fungal Lectin

Contact Info

Product

Resources

About