2bn0
From Proteopedia
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| , resolution 2.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
BANANA LECTIN BOUND TO LAMINARIBIOSE
Overview
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.
About this Structure
2BN0 is a Single protein structure of sequence from Musa acuminata. Full crystallographic information is available from OCA.
Reference
Crystal structure of banana lectin reveals a novel second sugar binding site., Meagher JL, Winter HC, Ezell P, Goldstein IJ, Stuckey JA, Glycobiology. 2005 Oct;15(10):1033-42. Epub 2005 Jun 8. PMID:15944373
Page seeded by OCA on Thu Mar 20 16:04:06 2008
