1Q8O

Pterocartpus angolensis lectin PAL in complex with the dimmanoside Man(alpha1-2)Man

Summary for 1Q8O

• Entry DOI: 10.2210/pdb1q8o/pdb
• Related: 1N3O 1N3P 1N3Q 1Q8P 1Q8Q 1Q8S 1Q8V 1UKG
• Descriptor: lectin, alpha-D-mannopyranose-(1-2)-methyl alpha-D-mannopyranoside, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: lectin, carbohydrate, mannose, sugar binding protein
• Biological source: Pterocarpus angolensis
• Total number of polymer chains: 2
• Total formula weight: 56019.27

Authors

Loris, R.,Van Walle, I.,De Greve, H.,Beeckmans, S.,Deboeck, F.,Wyns, L.,Bouckaert, J. (deposition date: 2003-08-22, release date: 2004-02-10, Last modification date: 2024-10-23)

Primary citation

Loris, R.,Van Walle, I.,De Greve, H.,Beeckmans, S.,Deboeck, F.,Wyns, L.,Bouckaert, J.
Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin
J.Mol.Biol., 335:1227-1240, 2004

PubMed Abstract: The crystal structure of a Man/Glc-specific lectin from the seeds of the bloodwood tree (Pterocarpus angolensis), a leguminous plant from central Africa, has been determined in complex with mannose and five manno-oligosaccharides. The lectin contains a classical mannose-specificity loop, but its metal-binding loop resembles that of lectins of unrelated specificity from Ulex europaeus and Maackia amurensis. As a consequence, the interactions with mannose in the primary binding site are conserved, but details of carbohydrate-binding outside the primary binding site differ from those seen in the equivalent carbohydrate complexes of concanavalin A. These observations explain the differences in their respective fine specificity profiles for oligomannoses. While Man(alpha1-3)Man and Man(alpha1-3)[Man(alpha1-6)]Man bind to PAL in low-energy conformations identical with that of ConA, Man(alpha1-6)Man is required to adopt a different conformation. Man(alpha1-2)Man can bind only in a single binding mode, in sharp contrast to ConA, which creates a higher affinity for this disaccharide by allowing two binding modes.

PubMed: 14729339
DOI: 10.1016/j.jmb.2003.11.043

Experimental method

X-RAY DIFFRACTION (2.2 Å)