View source for 1ur4


==The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products.==
<StructureSection load='1ur4' size='340' side='right'caption='[[1ur4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ur4]] 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=1UR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UR4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900113:4beta-beta-galactobiose'>PRD_900113</scene></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=1ur4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ur4 OCA], [https://pdbe.org/1ur4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ur4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ur4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ur4 ProSAT]</span></td></tr>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ur/1ur4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1ur4 ConSurf].
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== 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>
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<div class="pdbe-citations 1ur4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus licheniformis]]
[[Category: Large Structures]]
[[Category: Bjornvad M]]
[[Category: Christensen LLH]]
[[Category: Jorgensen CT]]
[[Category: Larsen S]]
[[Category: Le Nours J]]
[[Category: Lo Leggio L]]
[[Category: Ryttersgaard C]]