6ubb: Difference between revisions

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<StructureSection load='6ubb' size='340' side='right'caption='[[6ubb]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='6ubb' size='340' side='right'caption='[[6ubb]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ubb]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Aureobasidium_namibiae_cbs_147.97 Aureobasidium namibiae cbs 147.97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UBB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UBB FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ubb]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aureobasidium_namibiae_CBS_147.97 Aureobasidium namibiae CBS 147.97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UBB 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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M436DRAFT_66913 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1043004 Aureobasidium namibiae CBS 147.97])</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=PRD_900024:beta-laminaribiose'>PRD_900024</scene></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=6ubb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ubb OCA], [http://pdbe.org/6ubb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ubb RCSB], [http://www.ebi.ac.uk/pdbsum/6ubb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ubb ProSAT]</span></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=6ubb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ubb OCA], [https://pdbe.org/6ubb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ubb RCSB], [https://www.ebi.ac.uk/pdbsum/6ubb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ubb ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A074W9U7_9PEZI A0A074W9U7_9PEZI]
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>
==See Also==
 
*[[Glucanase 3D structures|Glucanase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ubb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aureobasidium namibiae cbs 147 97]]
[[Category: Aureobasidium namibiae CBS 147 97]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cordeiro, R L]]
[[Category: Cordeiro RL]]
[[Category: Domingues, M N]]
[[Category: Domingues MN]]
[[Category: Murakami, M T]]
[[Category: Murakami MT]]
[[Category: Santos, C R]]
[[Category: Santos CR]]
[[Category: Tomazini, A]]
[[Category: Tomazini A]]
[[Category: Vieira, P S]]
[[Category: Vieira PS]]
[[Category: Carbohydrate]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]

Latest revision as of 14:56, 13 March 2024

Crystal structure of a GH128 (subgroup VI) exo-beta-1,3-glucanase from Aureobasidium namibiae (AnGH128_VI) with laminaribiose at the surface-binding site

6ubb, resolution 2.35Å

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