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==Crystal structure of the E263A nucleophile mutant of Bacillus licheniformis endo-beta-1,4-galactanase in complex with galactotriose==
==Crystal structure of the E263A nucleophile mutant of Bacillus licheniformis endo-beta-1,4-galactanase in complex with galactotriose==
<StructureSection load='2gft' size='340' side='right' caption='[[2gft]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2gft' size='340' side='right'caption='[[2gft]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2gft]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GFT FirstGlance]. <br>
<table><tr><td colspan='2'>[[2gft]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GFT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ccr|2ccr]], [[1r8l|1r8l]], [[1ur0|1ur0]], [[1ur4|1ur4]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900114:4beta-beta-galactotriose'>PRD_900114</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinogalactan_endo-beta-1,4-galactanase Arabinogalactan endo-beta-1,4-galactanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.89 3.2.1.89] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gft OCA], [https://pdbe.org/2gft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gft RCSB], [https://www.ebi.ac.uk/pdbsum/2gft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gft ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gft OCA], [http://pdbe.org/2gft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gft RCSB], [http://www.ebi.ac.uk/pdbsum/2gft PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GANB_BACLD GANB_BACLD] Involved in galactan degradation (PubMed:15312766). Degrades arabinose-free galactan to galactooligosaccharides, producing galactotetraose as the main product along with galactotriose, galactobiose, and galactose (PubMed:15312766). May hydrolyze the beta-1,4-galactan linkages of the galactan portion of arabinogalactan type I, a pectic plant polysaccharide from which most of the arabinose has been removed (By similarity).[UniProtKB:O07013]<ref>PMID:15312766</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/2gft_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gf/2gft_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gft ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:15312766</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gft" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Clostridium licheniforme weigmann 1898]]
[[Category: Bacillus licheniformis]]
[[Category: Arabinogalactan endo-beta-1,4-galactanase]]
[[Category: Large Structures]]
[[Category: Christensen, L L.H]]
[[Category: Christensen LLH]]
[[Category: Jorgensen, C T]]
[[Category: De Maria L]]
[[Category: Larsen, S]]
[[Category: Jorgensen CT]]
[[Category: Leggio, L Lo]]
[[Category: Larsen S]]
[[Category: Maria, L De]]
[[Category: Le Nours J]]
[[Category: Nours, J Le]]
[[Category: Lo Leggio L]]
[[Category: Welner, D]]
[[Category: Welner D]]
[[Category: Beta-alpha-8-barrel]]
[[Category: Hydrolase]]
[[Category: Nucleophile inactive mutant]]
[[Category: Protein-oligosaccharide complex]]

Latest revision as of 12:27, 14 February 2024

Crystal structure of the E263A nucleophile mutant of Bacillus licheniformis endo-beta-1,4-galactanase in complex with galactotrioseCrystal structure of the E263A nucleophile mutant of Bacillus licheniformis endo-beta-1,4-galactanase in complex with galactotriose

Structural highlights

2gft is a 2 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GANB_BACLD Involved in galactan degradation (PubMed:15312766). Degrades arabinose-free galactan to galactooligosaccharides, producing galactotetraose as the main product along with galactotriose, galactobiose, and galactose (PubMed:15312766). May hydrolyze the beta-1,4-galactan linkages of the galactan portion of arabinogalactan type I, a pectic plant polysaccharide from which most of the arabinose has been removed (By similarity).[UniProtKB:O07013][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Ryttersgaard C, Le Nours J, Lo Leggio L, Jorgensen CT, Christensen LL, Bjornvad M, Larsen S. The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. J Mol Biol. 2004 Jul 30;341(1):107-17. PMID:15312766 doi:http://dx.doi.org/10.1016/j.jmb.2004.05.017

2gft, resolution 2.30Å

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