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 Cited by 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: 30065388DOI: 10.1038/s41598-018-29439-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.749 Å) |
Structure validation
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