View source for 2ccr

==STRUCTURE OF BETA-1,4-GALACTANASE==
<StructureSection load='2ccr' size='340' side='right' caption='[[2ccr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ccr]] is a 2 chain structure with sequence 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=2CCR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CCR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B2G:GALACTOBIOSE'>B2G</scene>, <scene name='pdbligand=B4G:GALACTOTRIOSE'>B4G</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ur0|1ur0]], [[1ur4|1ur4]]</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-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></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=2ccr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ccr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ccr RCSB], [http://www.ebi.ac.uk/pdbsum/2ccr PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/GANA_BACLD GANA_BACLD]] Hydrolyzes the beta-1,4-galactan linkages of arabinogalactan type I, a pectic substance found in plants such as soybeans. 
== 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/cc/2ccr_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microbial beta-1,4-galactanases are glycoside hydrolases belonging to family 53, which degrade galactan and arabinogalactan side chains in the hairy regions of pectin, a major plant cell wall component. They belong to the larger clan GH-A of glycoside hydrolases, which cover many different poly- and oligosaccharidase specificities. Crystallographic complexes of Bacillus licheniformis beta-1,4-galactanase and its inactive nucleophile mutant have been obtained with methyl-beta(1--&gt;4)-galactotetraoside, providing, for the first time, information on substrate binding to the aglycone side of the beta-1,4-galactanase substrate binding groove. Using the experimentally determined subsites as a starting point, a beta(1--&gt;4)-galactononaose was built into the structure and subjected to molecular dynamics simulations giving further insight into the residues involved in the binding of the polysaccharide from subsite -4 to +5. In particular, this analysis newly identified a conserved beta-turn, which contributes to subsites -2 to +3. This beta-turn is unique to family 53 beta-1,4-galactanases among all clan GH-A families that have been structurally characterized and thus might be a structural signature for endo-beta-1,4-galactanase specificity.

Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling.,Le Nours J, De Maria L, Welner D, Jorgensen CT, Christensen LL, Borchert TV, Larsen S, Lo Leggio L Proteins. 2009 Jun;75(4):977-89. PMID:19089956<ref>PMID:19089956</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Beta-1%2C4-galactanase|Beta-1%2C4-galactanase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabinogalactan endo-1,4-beta-galactosidase]]
[[Category: Bacillus licheniformis]]
[[Category: Christensen, L L.H]]
[[Category: Jorgensen, C T]]
[[Category: Larsen, S]]
[[Category: Leggio, L Lo]]
[[Category: Maria, L De]]
[[Category: Nours, J Le]]
[[Category: Welner, D]]
[[Category: 4-galactanase]]
[[Category: Beta-1]]
[[Category: Galactan]]
[[Category: Gh-a]]
[[Category: Glycoside hydrolase family 53]]
[[Category: Hydrolase]]