6uay
From Proteopedia
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<StructureSection load='6uay' size='340' side='right'caption='[[6uay]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6uay' size='340' side='right'caption='[[6uay]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UAY FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=6uay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uay OCA], [https://pdbe.org/6uay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uay RCSB], [https://www.ebi.ac.uk/pdbsum/6uay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uay ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The fundamental and assorted roles of beta-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of action of a glycoside hydrolase family active on beta-1,3-glucans were systematically investigated combining sequence similarity network, phylogeny, X-ray crystallography, enzyme kinetics, mutagenesis and molecular dynamics. This family exhibits a minimalist and versatile (alpha/beta)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical beta-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of beta-1,3-glucans or through a substrate conformational change imposed by the active-site topology of some fungal enzymes. Together, these findings expand our understanding of the enzymatic arsenal of bacteria and fungi for the breakdown and modification of beta-1,3-glucans, which can be exploited for biotechnological applications. | ||
- | + | ==See Also== | |
- | + | *[[Glucanase 3D structures|Glucanase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Blastomyces gilchristii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Costa | + | [[Category: Costa PACR]] |
- | [[Category: Domingues | + | [[Category: Domingues MN]] |
- | [[Category: Lima | + | [[Category: Lima EA]] |
- | [[Category: Mandelli | + | [[Category: Mandelli F]] |
- | [[Category: Murakami | + | [[Category: Murakami MT]] |
- | [[Category: Santos | + | [[Category: Santos CR]] |
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Current revision
Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta-1,3-glucanase from Blastomyces gilchristii (BgGH128_III)
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