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6uaq

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Current revision (14:56, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6uaq' size='340' side='right'caption='[[6uaq]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='6uaq' size='340' side='right'caption='[[6uaq]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6uaq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_mediterranei"_margalith_and_beretta_1960 "streptomyces mediterranei" margalith and beretta 1960]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UAQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UAQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6uaq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_mediterranei Amycolatopsis mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UAQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6uaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uaq OCA], [http://pdbe.org/6uaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uaq RCSB], [http://www.ebi.ac.uk/pdbsum/6uaq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uaq ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6uaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uaq OCA], [https://pdbe.org/6uaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uaq RCSB], [https://www.ebi.ac.uk/pdbsum/6uaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uaq ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G0FQ07_AMYMS G0FQ07_AMYMS]
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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.
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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>
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6uaq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Streptomyces mediterranei margalith and beretta 1960]]
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[[Category: Amycolatopsis mediterranei]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Costa, P A.C R]]
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[[Category: Costa PACR]]
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[[Category: Murakami, M T]]
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[[Category: Murakami MT]]
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[[Category: Santos, C R]]
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[[Category: Santos CR]]
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[[Category: Carbohydrate]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Hydrolase]]
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Current revision

Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I)

PDB ID 6uaq

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