6FLY

Structure of AcmJRL, a mannose binding jacalin related lectin from Ananas comosus, in complex with mannose.

Summary for 6FLY

• Entry DOI: 10.2210/pdb6fly/pdb
• Related: 6FLW
• Descriptor: Jacalin-like lectin, alpha-D-mannopyranose (3 entities in total)
• Functional Keywords: mannose binding lectin, a. comosus stem, sugar binding protein
• Biological source: Ananas comosus (Pineapple)
• Total number of polymer chains: 2
• Total formula weight: 31441.35

Authors

Azarkan, M.,Herman, R.,El Mahyaoui, R.,Sauvage, E.,Vanden Broeck, A.,Charlier, P. (deposition date: 2018-01-29, release date: 2018-08-15, Last modification date: 2024-01-17)

Primary citation

Azarkan, M.,Feller, G.,Vandenameele, J.,Herman, R.,El Mahyaoui, R.,Sauvage, E.,Vanden Broeck, A.,Matagne, A.,Charlier, P.,Kerff, F.
Biochemical and structural characterization of a mannose binding jacalin-related lectin with two-sugar binding sites from pineapple (Ananas comosus) stem.
Sci Rep, 8:11508-11508, 2018

PubMed Abstract: A mannose binding jacalin-related lectin from Ananas comosus stem (AcmJRL) was purified and biochemically characterized. This lectin is homogeneous according to native, SDS-PAGE and N-terminal sequencing and the theoretical molecular mass was confirmed by ESI-Q-TOF-MS. AcmJRL was found homodimeric in solution by size-exclusion chromatography. Rat erythrocytes are agglutinated by AcmJRL while no agglutination activity is detected against rabbit and sheep erythrocytes. Hemagglutination activity was found more strongly inhibited by mannooligomannosides than by D-mannose. The carbohydrate-binding specificity of AcmJRL was determined in some detail by isothermal titration calorimetry. All sugars tested were found to bind with low affinity to AcmJRL, with K values in the mM range. In agreement with hemagglutination assays, the affinity increased from D-mannose to di-, tri- and penta-mannooligosaccharides. Moreover, the X-ray crystal structure of AcmJRL was obtained in an apo form as well as in complex with D-mannose and methyl-α-D-mannopyranoside, revealing two carbohydrate-binding sites per monomer similar to the banana lectin BanLec. The absence of a wall separating the two binding sites, the conformation of β7β8 loop and the hemagglutinating activity are reminiscent of the BanLec His84Thr mutant, which presents a strong anti-HIV activity in absence of mitogenic activity.

PubMed: 30065388
DOI: 10.1038/s41598-018-29439-x

Experimental method

X-RAY DIFFRACTION (2.749 Å)