View source for 1ur0

[[Image:1ur0.gif|left|200px]]<br /><applet load="1ur0" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1ur0, resolution 2.50&Aring;" />
'''THE STRUCTURE OF ENDO-BETA-1,4-GALACTANASE FROM BACILLUS LICHENIFORMIS IN COMPLEX WITH TWO OLIGOSACCHARIDE PRODUCTS.'''<br />

==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 disulphide, bridge in the fungal galactanases. Compared to the substrate-binding, subsites predicted for Aspergillus aculeatus galactanase (AAGAL), two, additional subsites for substrate binding are found in BLGAL, -3 and -4. A, comparison of the pattern of galactan and galactooligosaccharides, degradation by AAGAL and BLGAL shows that, although both are most active, on substrates with a high degree of polymerization, AAGAL can degrade, galactotriose and galactotetraose efficiently, whereas BLGAL prefers, longer oligosaccharides and cannot hydrolyze galactotriose to any, appreciable extent. This difference in substrate preference can be, explained structurally by the presence of the extra subsites -3 and -4 in, BLGAL.

==About this Structure==
1UR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with B4G, CA and PGE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arabinogalactan_endo-1,4-beta-galactosidase Arabinogalactan endo-1,4-beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.89 3.2.1.89] Known structural/functional Site: <scene name='pdbsite=AC1:B4g Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UR0 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15312766 15312766]
[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
[[Category: Bacillus licheniformis]]
[[Category: Single protein]]
[[Category: Bjornvad, M.]]
[[Category: Christensen, L.L.H.]]
[[Category: Jorgensen, C.]]
[[Category: Larsen, S.]]
[[Category: Leggio, L.Lo.]]
[[Category: Nours, J.Le.]]
[[Category: Ryttersgaard, C.]]
[[Category: B4G]]
[[Category: CA]]
[[Category: PGE]]
[[Category: 4-galactanase]]
[[Category: beta-1]]
[[Category: family 53]]
[[Category: gh-a]]
[[Category: glycoside hydrolase]]
[[Category: pectin]]
[[Category: plant cell wall degradation]]
[[Category: substrate specificity]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:07:48 2007''