2bn0

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[[Category: mannose-specific jacalin-related lectin]]
[[Category: mannose-specific jacalin-related lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:29:00 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:42:57 2007''

Revision as of 14:38, 30 October 2007


2bn0, resolution 2.80Å

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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 ... [(full description)]

About this Structure

2BN0 is a [Single protein] structure of sequence from [Musa acuminata] with CD and SO4 as [ligands]. Structure known Active Site: AC1. 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

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