2BN0

Banana Lectin bound to Laminaribiose

Summary for 2BN0

• Entry DOI: 10.2210/pdb2bn0/pdb
• Related: 2BMY 2BMZ
• Related PRD ID: PRD_900024
• Descriptor: RIPENING-ASSOCIATED PROTEIN, beta-D-glucopyranose-(1-3)-beta-D-glucopyranose, CADMIUM ION, ... (5 entities in total)
• Functional Keywords: mannose-specific jacalin-related lectin, sugar binding protein
• Biological source: MUSA ACUMINATA (BANANA)
• Total number of polymer chains: 2
• Total formula weight: 30844.90

Authors

Meagher, J.L.,Winter, H.C.,Ezell, P.,Goldstein, I.J.,Stuckey, J.A. (deposition date: 2005-03-17, release date: 2005-06-16, Last modification date: 2023-12-13)

Primary citation

Meagher, J.L.,Winter, H.C.,Ezell, P.,Goldstein, I.J.,Stuckey, J.A.
Crystal Structure of Banana Lectin Reveals a Novel Second Sugar Binding Site.
Glycobiology, 15:1033-, 2005

PubMed Abstract: Banana lectin (Banlec) is a dimeric plant lectin from the jacalin-related lectin family. Banlec belongs to a subgroup of this family that binds to glucose/mannose, but is unique in recognizing internal alpha1,3 linkages as well as beta1,3 linkages at the reducing termini. Here we present the crystal structures of Banlec alone and with laminaribiose (LAM) (Glcbeta1, 3Glc) and Xyl-beta1,3-Man-alpha-O-Methyl. The structure of Banlec has a beta-prism-I fold, similar to other family members, but differs from them in its mode of sugar binding. The reducing unit of the sugar is inserted into the binding site causing the second saccharide unit to be placed in the opposite orientation compared with the other ligand-bound structures of family members. More importantly, our structures reveal the presence of a second sugar binding site that has not been previously reported in the literature. The residues involved in the second site are common to other lectins in this family, potentially signaling a new group of mannose-specific jacalin-related lectins (mJRL) with two sugar binding sites.

PubMed: 15944373
DOI: 10.1093/GLYCOB/CWI088

Experimental method

X-RAY DIFFRACTION (2.8 Å)