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6jql

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Structure of PaaZ, a bifunctional enzyme

6jql, resolution 2.90Å

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Retrieved from "http://52.214.119.220/wiki/index.php/6jql"

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 <SX load='6jql' size='340' side='right' viewer='molstar' caption='[[6jql]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6jql]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JQL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6jql]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQL FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paaZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxepin-CoA_hydrolase Oxepin-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.12 3.3.2.12] </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=6jql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jql OCA], [https://pdbe.org/6jql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jql RCSB], [https://www.ebi.ac.uk/pdbsum/6jql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jql ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jql OCA], [http://pdbe.org/6jql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jql RCSB], [http://www.ebi.ac.uk/pdbsum/6jql PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jql ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PAAZ_ECOLI PAAZ_ECOLI]] Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.<ref>PMID:20660314</ref> <ref>PMID:21296885</ref> <ref>PMID:9748275</ref>
+[https://www.uniprot.org/uniprot/PAAZ_ECOLI PAAZ_ECOLI] Catalyzes the hydrolytic ring cleavage of 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) via the open-chain aldehyde intermediate to yield 3-oxo-5,6-dehydrosuberyl-CoA. The enzyme consists of a C-terminal (R)-specific enoyl-CoA hydratase domain (formerly MaoC) that cleaves the ring and produces the highly reactive 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde and an N-terminal NADP-dependent aldehyde dehydrogenase domain that oxidizes the aldehyde to 3-oxo-5,6-dehydrosuberyl-CoA. Can also use crotonyl-CoA as substrate.<ref>PMID:20660314</ref> <ref>PMID:21296885</ref> <ref>PMID:9748275</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Substrate channeling is a mechanism for the internal transfer of hydrophobic, unstable or toxic intermediates from the active site of one enzyme to another. Such transfer has previously been described to be mediated by a hydrophobic tunnel, the use of electrostatic highways or pivoting and by conformational changes. The enzyme PaaZ is used by many bacteria to degrade environmental pollutants. PaaZ is a bifunctional enzyme that catalyzes the ring opening of oxepin-CoA and converts it to 3-oxo-5,6-dehydrosuberyl-CoA. Here we report the structures of PaaZ determined by electron cryomicroscopy with and without bound ligands. The structures reveal that three domain-swapped dimers of the enzyme form a trilobed structure. A combination of small-angle X-ray scattering (SAXS), computational studies, mutagenesis and microbial growth experiments suggests that the key intermediate is transferred from one active site to the other by a mechanism of electrostatic pivoting of the CoA moiety, mediated by a set of conserved positively charged residues.
-Molecular basis for metabolite channeling in a ring opening enzyme of the phenylacetate degradation pathway.,Sathyanarayanan N, Cannone G, Gakhar L, Katagihallimath N, Sowdhamini R, Ramaswamy S, Vinothkumar KR Nat Commun. 2019 Sep 11;10(1):4127. doi: 10.1038/s41467-019-11931-1. PMID:31511507<ref>PMID:31511507</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6jql" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Oxepin-CoA hydrolase]]
+[[Category: Cannone G]]
-[[Category: Cannone, G]]
+[[Category: Gakher L]]
-[[Category: Gakher, L]]
+[[Category: Katagihallimath N]]
-[[Category: Katagihallimath, N]]
+[[Category: Sathyanarayanan N]]
-[[Category: Sathyanarayanan, N]]
+[[Category: Sowdhamini R]]
-[[Category: Sowdhamini, R]]
+[[Category: Vinothkumar KR]]
-[[Category: Vinothkumar, K R]]
-[[Category: Bi-functional enzyme]]
-[[Category: Dehydrogenase]]
-[[Category: Hydrolase]]
-[[Category: Substrate channeling]]

6jql

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Structure of PaaZ, a bifunctional enzyme

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