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5bwi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystallographic structure of a bacterial heparanase== | |
| + | <StructureSection load='5bwi' size='340' side='right'caption='[[5bwi]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5bwi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BWI 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5bwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bwi OCA], [https://pdbe.org/5bwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bwi RCSB], [https://www.ebi.ac.uk/pdbsum/5bwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bwi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q63T97_BURPS Q63T97_BURPS] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We report the structural and functional characterization of a novel heparanase (BpHep) from the invasive pathogenic bacterium Burkholderia pseudomallei (Bp), showing approximately 24% sequence identity with human heparanase (hHep). Site-directed mutagenesis studies confirmed the active site resi-dues essential for activity, and we found that BpHep has specificity for heparan sulfate. Finally, we describe the first heparanase X-ray crystal structure, which provides new insight into both substrate recognition and inhibitor design. | ||
| - | + | Functional and structural characterization of a heparanase.,Bohlmann L, Tredwell GD, Yu X, Chang CW, Haselhorst T, Winger M, Dyason JC, Thomson RJ, Tiralongo J, Beacham IR, Blanchard H, von Itzstein M Nat Chem Biol. 2015 Dec;11(12):955-7. doi: 10.1038/nchembio.1956. Epub 2015 Nov, 2. PMID:26565989<ref>PMID:26565989</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Blanchard | + | <div class="pdbe-citations 5bwi" style="background-color:#fffaf0;"></div> |
| - | [[Category: Yu | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Burkholderia pseudomallei]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Blanchard H]] | ||
| + | [[Category: Yu X]] | ||
Current revision
Crystallographic structure of a bacterial heparanase
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