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3ro8

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<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=3ro8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ro8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ro8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ro8 PDBsum]</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=3ro8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ro8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ro8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ro8 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/XYNA1_PAESJ XYNA1_PAESJ]] Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues, which is predominant in hemicellulose fractions of hardwood and crop residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the predominant products of MeGAXn hydrolysis; these products are then directly assimilated by the bacterium for subsequent metabolism. Thus, allows the bacterium to efficiently use polymeric MeGAXn as a growth substrate.<ref>PMID:16461704</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 10:08, 25 December 2014

Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2

3ro8, resolution 1.34Å

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