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3ro8

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==Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2==
==Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2==
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<StructureSection load='3ro8' size='340' side='right' caption='[[3ro8]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
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<StructureSection load='3ro8' size='340' side='right'caption='[[3ro8]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ro8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Paesj Paesj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RO8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ro8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Paesj Paesj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RO8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rdk|3rdk]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rdk|3rdk]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pjdr2_0221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=324057 PAESJ])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pjdr2_0221 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=324057 PAESJ])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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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://pdbe.org/3ro8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ro8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ro8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ro8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ro8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ro8 OCA], [https://pdbe.org/3ro8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ro8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ro8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ro8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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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[[https://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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
[[Category: Paesj]]
[[Category: Paesj]]
[[Category: John, F J.St]]
[[Category: John, F J.St]]

Revision as of 10:19, 22 June 2022

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

PDB ID 3ro8

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