1ofz

From Proteopedia

Revision as of 13:48, 30 October 2007

CRYSTAL STRUCTURE OF FUNGAL LECTIN: SIX-BLADED BETA-PROPELLER FOLD AND NOVEL FUCOSE RECOGNITION MODE FOR ALEURIA AURANTIA LECTIN

Overview

Aleuria aurantia lectin is a fungal protein composed of two identical, 312-amino acid subunits that specifically recognizes fucosylated glycans., The crystal structure of the lectin complexed with fucose reveals that, each monomer consists of a six-bladed beta-propeller fold and of a small, antiparallel two-stranded beta-sheet that plays a role in dimerization., Five fucose residues were located in binding pockets between the adjacent, propeller blades. Due to repeats in the amino acid sequence, there are, strong similarities between the sites. Oxygen atoms O-3, O-4, and O-5 of, fucose are involved in hydrogen bonds with side chains of amino acids, conserved in all repeats, whereas O-1 and O-2 interact with a large number, of water molecules. The nonpolar face of each fucose residue is ... [(full description)]

About this Structure

1OFZ is a [Single protein] structure of sequence from [Aleuria aurantia] with FUL and FUC as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria aurantia lectin., Wimmerova M, Mitchell E, Sanchez JF, Gautier C, Imberty A, J Biol Chem. 2003 Jul 18;278(29):27059-67. Epub 2003 May 5. PMID:12732625

Page seeded by OCA on Tue Oct 30 15:52:59 2007