1N3Q

Pterocarpus angolensis lectin complexed with turanose

Summary for 1N3Q

• Entry DOI: 10.2210/pdb1n3q/pdb
• Related: 1N3O 1N3P
• Related PRD ID: PRD_900047
• Descriptor: lectin PAL, alpha-D-glucopyranose-(1-3)-beta-D-fructofuranose, alpha-D-glucopyranose-(1-3)-beta-D-fructopyranose, ... (6 entities in total)
• Functional Keywords: lectin, carbohydrate recognition, turanose, sugar binding protein
• Biological source: Pterocarpus angolensis
• Total number of polymer chains: 2
• Total formula weight: 56025.28

Authors

Loris, R.,Imberty, A.,Beeckmans, S.,Van Driessche, E.,Read, J.S.,Bouckaert, J.,De Greve, H.,Buts, L.,Wyns, L. (deposition date: 2002-10-29, release date: 2002-11-20, Last modification date: 2024-03-13)

Primary citation

Loris, R.,Imberty, A.,Beeckmans, S.,Van Driessche, E.,Read, J.S.,Bouckaert, J.,De Greve, H.,Buts, L.,Wyns, L.
Crystal structure of Pterocarpus angolensis lectin in complex with glucose, sucrose, and turanose
J.BIOL.CHEM., 278:16297-16303, 2003

PubMed Abstract: The crystal structure of the Man/Glc-specific seed lectin from Pterocarpus angolensis was determined in complex with methyl-alpha-d-glucose, sucrose, and turanose. The carbohydrate binding site contains a classic Man/Glc type specificity loop. Its metal binding loop on the other hand is of the long type, different from what is observed in other Man/Glc-specific legume lectins. Glucose binding in the primary binding site is reminiscent of the glucose complexes of concanavalin A and lentil lectin. Sucrose is found to be bound in a conformation similar as seen in the binding site of lentil lectin. A direct hydrogen bond between Ser-137(OG) to Fru(O2) in Pterocarpus angolensis lectin replaces a water-mediated interaction in the equivalent complex of lentil lectin. In the turanose complex, the binding site of the first molecule in the asymmetric unit contains the alphaGlc1-3betaFruf form of furanose while the second molecule contains the alphaGlc1-3betaFrup form in its binding site.

PubMed: 12595543
DOI: 10.1074/jbc.M211148200

Experimental method

X-RAY DIFFRACTION (2.2 Å)