3rdk
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Protein crystal structure of xylanase A1 of Paenibacillus sp. JDR-2== |
+ | <StructureSection load='3rdk' size='340' side='right' caption='[[3rdk]], [[Resolution|resolution]] 1.49Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3rdk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Paenibacillus_sp._jdr-2 Paenibacillus sp. jdr-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RDK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RDK FirstGlance]. <br> | ||
+ | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene>, <scene name='pdbligand=GCV:4-O-METHYL-ALPHA-D-GLUCURONIC+ACID'>GCV</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr> | ||
+ | <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 Paenibacillus sp. JDR-2])</td></tr> | ||
+ | <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> | ||
+ | <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=3rdk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rdk RCSB], [http://www.ebi.ac.uk/pdbsum/3rdk PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Gram-positive bacterium Paenibacillus sp. JDR-2 (PbJDR2) has been shown to have novel properties in the utilization of the abundant but chemically complex hemicellulosic sugar glucuronoxylan. Xylanase A1 of PbJDR2 (PbXynA1) has been implicated in an efficient process in which extracellular depolymerization of this polysaccharide is coupled to assimilation and intracellular metabolism. PbXynA1is a 154kDa cell wall anchored multimodular glycosyl hydrolase family 10 (GH10) xylanase. In this work, the 38kDa catalytic module of PbXynA1 has been structurally characterized revealing several new features not previously observed in structures of GH10 xylanases. These features are thought to facilitate hydrolysis of highly substituted, chemically complex xylans that may be the form found in close proximity to the cell wall of PbJDR2, an organism shown to have a preference for growth on polymeric glucuronoxylan. | ||
- | + | Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2.,St John FJ, Preston JF, Pozharski E J Struct Biol. 2012 Sep 18. pii: S1047-8477(12)00249-3. doi:, 10.1016/j.jsb.2012.09.007. PMID:23000703<ref>PMID:23000703</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | + | </StructureSection> | |
[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Paenibacillus sp. jdr-2]] | [[Category: Paenibacillus sp. jdr-2]] | ||
- | [[Category: John, F J.St | + | [[Category: John, F J.St]] |
- | [[Category: Pozharski, E | + | [[Category: Pozharski, E]] |
[[Category: Gh10]] | [[Category: Gh10]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Xylanase]] | [[Category: Xylanase]] |
Revision as of 13:10, 9 December 2014
Protein crystal structure of xylanase A1 of Paenibacillus sp. JDR-2
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