6ub5: Difference between revisions
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==Crystal structure (P21 form) of a GH128 (subgroup IV) endo-beta-1,3-glucanase from Lentinula edodes (LeGH128_IV) in complex with laminaritriose== | |||
<StructureSection load='6ub5' size='340' side='right'caption='[[6ub5]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ub5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lened Lened]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UB5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UB5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glu1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5353 LENED])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ub5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ub5 OCA], [http://pdbe.org/6ub5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ub5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ub5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ub5 ProSAT]</span></td></tr> | |||
</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. | |||
Structural insights into beta-1,3-glucan cleavage by a glycoside hydrolase family.,Santos CR, Costa PACR, Vieira PS, Gonzalez SET, Correa TLR, Lima EA, Mandelli F, Pirolla RAS, Domingues MN, Cabral L, Martins MP, Cordeiro RL, Junior AT, Souza BP, Prates ET, Gozzo FC, Persinoti GF, Skaf MS, Murakami MT Nat Chem Biol. 2020 May 25. pii: 10.1038/s41589-020-0554-5. doi:, 10.1038/s41589-020-0554-5. PMID:32451508<ref>PMID:32451508</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ub5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lened]] | |||
[[Category: Lima, E A]] | |||
[[Category: Mandelli, F]] | |||
[[Category: Murakami, M T]] | |||
[[Category: Santos, C R]] | |||
[[Category: Carbohydrate]] | |||
[[Category: Glycosyl hydrolase]] | |||
[[Category: Hydrolase]] | |||