1r8l

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[[Image:1r8l.gif|left|200px]]
[[Image:1r8l.gif|left|200px]]
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{{Structure
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|PDB= 1r8l |SIZE=350|CAPTION= <scene name='initialview01'>1r8l</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1r8l", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1r8l| PDB=1r8l | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r8l OCA], [http://www.ebi.ac.uk/pdbsum/1r8l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r8l RCSB]</span>
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'''The structure of endo-beta-1,4-galactanase from Bacillus licheniformis'''
'''The structure of endo-beta-1,4-galactanase from Bacillus licheniformis'''
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==About this Structure==
==About this Structure==
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1R8L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8L OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8L OCA].
==Reference==
==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://www.ncbi.nlm.nih.gov/pubmed/15312766 15312766]
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://www.ncbi.nlm.nih.gov/pubmed/15312766 15312766]
[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
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[[Category: Bacillus licheniformis]]
 
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[[Category: Protein complex]]
 
[[Category: Bjornvad, M.]]
[[Category: Bjornvad, M.]]
[[Category: Christensen, L L.]]
[[Category: Christensen, L L.]]
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[[Category: Nours, J Le.]]
[[Category: Nours, J Le.]]
[[Category: Ryttersgaard, C.]]
[[Category: Ryttersgaard, C.]]
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[[Category: (beta-alpha)8-barrel]]
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[[Category: Calcium ion]]
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[[Category: calcium ion]]
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[[Category: Clan gh-a]]
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[[Category: clan gh-a]]
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[[Category: Family 53]]
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[[Category: family 53]]
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[[Category: Glycosyl hydrolase]]
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[[Category: glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:13:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:24:44 2008''
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Revision as of 04:13, 3 May 2008

Template:STRUCTURE 1r8l

The structure of endo-beta-1,4-galactanase from Bacillus licheniformis


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

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 Sat May 3 07:13:08 2008

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