1ur4
From Proteopedia
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|PDB= 1ur4 |SIZE=350|CAPTION= <scene name='initialview01'>1ur4</scene>, resolution 2.20Å | |PDB= 1ur4 |SIZE=350|CAPTION= <scene name='initialview01'>1ur4</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=AC1:B2g+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:B2g+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=B2G:GALACTOBIOSE'>B2G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=B2G:GALACTOBIOSE'>B2G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ur4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur4 OCA], [http://www.ebi.ac.uk/pdbsum/1ur4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ur4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Nours, J Le.]] | [[Category: Nours, J Le.]] | ||
[[Category: Ryttersgaard, C.]] | [[Category: Ryttersgaard, C.]] | ||
| - | [[Category: B2G]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: PGE]] | ||
[[Category: 4-galactanase]] | [[Category: 4-galactanase]] | ||
[[Category: beta-1]] | [[Category: beta-1]] | ||
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[[Category: substrate specificity]] | [[Category: substrate specificity]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:02 2008'' |
Revision as of 21:14, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Activity: | Arabinogalactan endo-1,4-beta-galactosidase, with EC number 3.2.1.89 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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
1UR4 is a Single protein structure of sequence from Bacillus licheniformis. 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
Page seeded by OCA on Mon Mar 31 00:14:02 2008
Categories: Arabinogalactan endo-1,4-beta-galactosidase | Bacillus licheniformis | Single protein | Bjornvad, M. | Christensen, L L.H. | Jorgensen, C. | Larsen, S. | Leggio, L Lo. | Nours, J Le. | Ryttersgaard, C. | 4-galactanase | Beta-1 | Family 53 | Gh-a | Glycoside hydrolase | Pectin | Plant cell wall degradation | Substrate specificity
