7qe2

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7qe2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QE2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7qe2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QE2 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.15&#8491;</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BDP:BETA-D-GLUCOPYRANURONIC+ACID'>BDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7qe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qe2 OCA], [https://pdbe.org/7qe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7qe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qe2 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=7qe2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qe2 OCA], [https://pdbe.org/7qe2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qe2 RCSB], [https://www.ebi.ac.uk/pdbsum/7qe2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qe2 ProSAT]</span></td></tr>
</table>
</table>
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The abundance of recorded protein sequence data stands in contrast to the small number of experimentally verified functional annotation. Here we screened a million-membered metagenomic library at ultrahigh throughput in microfluidic droplets for beta-glucuronidase activity. We identified SN243, a genuine beta-glucuronidase with little homology to previously studied enzymes of this type, as a glycoside hydrolase 3 family member. This glycoside hydrolase family contains only one recently added beta-glucuronidase, showing that a functional metagenomic approach can shed light on assignments that are currently 'unpredictable' by bioinformatics. Kinetic analyses of SN243 characterized it as a promiscuous catalyst and structural analysis suggests regions of divergence from homologous glycoside hydrolase 3 members creating a wide-open active site. With a screening throughput of &gt;10(7) library members per day, picolitre-volume microfluidic droplets enable functional assignments that complement current enzyme database dictionaries and provide bridgeheads for the annotation of unexplored sequence space.
The abundance of recorded protein sequence data stands in contrast to the small number of experimentally verified functional annotation. Here we screened a million-membered metagenomic library at ultrahigh throughput in microfluidic droplets for beta-glucuronidase activity. We identified SN243, a genuine beta-glucuronidase with little homology to previously studied enzymes of this type, as a glycoside hydrolase 3 family member. This glycoside hydrolase family contains only one recently added beta-glucuronidase, showing that a functional metagenomic approach can shed light on assignments that are currently 'unpredictable' by bioinformatics. Kinetic analyses of SN243 characterized it as a promiscuous catalyst and structural analysis suggests regions of divergence from homologous glycoside hydrolase 3 members creating a wide-open active site. With a screening throughput of &gt;10(7) library members per day, picolitre-volume microfluidic droplets enable functional assignments that complement current enzyme database dictionaries and provide bridgeheads for the annotation of unexplored sequence space.
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Functional metagenomic screening identifies an unexpected beta-glucuronidase.,Neun S, Brear P, Campbell E, Tryfona T, El Omari K, Wagner A, Dupree P, Hyvonen M, Hollfelder F Nat Chem Biol. 2022 Oct;18(10):1096-1103. doi: 10.1038/s41589-022-01071-x. Epub, 2022 Jul 7. PMID:35799064<ref>PMID:35799064</ref>
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Functional metagenomic screening identifies an unexpected beta-glucuronidase.,Neun S, Brear P, Campbell E, Tryfona T, El Omari K, Wagner A, Dupree P, Hyvonen M, Hollfelder F Nat Chem Biol. 2022 Oct;18(10):1096-1103. doi: 10.1038/s41589-022-01071-x. Epub , 2022 Jul 7. PMID:35799064<ref>PMID:35799064</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

Current revision

Crystal structure of D-glucuronic acid bound to SN243

PDB ID 7qe2

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