1ur4

From Proteopedia

Revision as of 14:04, 30 October 2007

THE STRUCTURE OF ENDO-BETA-1,4-GALACTANASE FROM BACILLUS LICHENIFORMIS IN COMPLEX WITH TWO OLIGOSACCHARIDE PRODUCTS.

Overview

The beta-1,4-galactanase from Bacillus licheniformis (BLGAL) is a plant, cell-wall-degrading enzyme involved in the hydrolysis of beta-1,4-galactan, in the hairy regions of pectin. The crystal structure of BLGAL was, determined by molecular replacement both alone and in complex with the, products galactobiose and galactotriose, catching a first crystallographic, glimpse of fragments of beta-1,4-galactan. As expected for an enzyme, belonging to GH-53, the BLGAL structure reveals a (betaalpha)(8)-barrel, architecture. However, BLGAL betaalpha-loops 2, 7 and 8 are long in, contrast to the corresponding loops in structures of fungal galactanases, determined previously. The structure of BLGAL additionally shows a calcium, ion linking the long betaalpha-loops 7 and 8, which replaces a ... [(full description)]

About this Structure

1UR4 is a [Single protein] structure of sequence from [Bacillus licheniformis] with B2G, CA, PGE and PEG as [ligands]. Active as [Arabinogalactan endo-1,4-beta-galactosidase], with EC number [3.2.1.89]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products., Ryttersgaard C, Le Nours J, Lo Leggio L, Jorgensen CT, Christensen LL, Bjornvad M, Larsen S, J Mol Biol. 2004 Jul 30;341(1):107-17. PMID:15312766

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