6mfd: Difference between revisions
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The | ==GphF GNAT-like decarboxylase in complex with isobutyryl-CoA== | ||
<StructureSection load='6mfd' size='340' side='right'caption='[[6mfd]], [[Resolution|resolution]] 2.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mfd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archangium_violaceum Archangium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.794Å</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=CO6:ISOBUTYRYL-COENZYME+A'>CO6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6mfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfd OCA], [https://pdbe.org/6mfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfd RCSB], [https://www.ebi.ac.uk/pdbsum/6mfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/U6BSB2_9DELT U6BSB2_9DELT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Natural product biosynthetic pathways are replete with enzymes repurposed for new catalytic functions. In some modular polyketide synthase (PKS) pathways, a GCN5-related N-acetyltransferase (GNAT)-like enzyme with an additional decarboxylation function initiates biosynthesis. Here, we probe two PKS GNAT-like domains for the dual activities of S-acyl transfer from coenzyme A (CoA) to an acyl carrier protein (ACP) and decarboxylation. The GphF and CurA GNAT-like domains selectively decarboxylate substrates that yield the anticipated pathway starter units. The GphF enzyme lacks detectable acyl transfer activity, and a crystal structure with an isobutyryl-CoA product analog reveals a partially occluded acyltransfer acceptor site. Further analysis indicates that the CurA GNAT-like domain also catalyzes only decarboxylation, and the initial acyl transfer is catalyzed by an unidentified enzyme. Thus, PKS GNAT-like domains are re-classified as GNAT-like decarboxylases. Two other decarboxylases, malonyl-CoA decarboxylase and EryM, reside on distant nodes of the superfamily, illustrating the adaptability of the GNAT fold. | |||
Repurposing the GNAT Fold in the Initiation of Polyketide Biosynthesis.,Skiba MA, Tran CL, Dan Q, Sikkema AP, Klaver Z, Gerwick WH, Sherman DH, Smith JL Structure. 2020 Jan 7;28(1):63-74.e4. doi: 10.1016/j.str.2019.11.004. Epub 2019, Nov 27. PMID:31785925<ref>PMID:31785925</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6mfd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Archangium violaceum]] | |||
[[Category: Large Structures]] | |||
[[Category: Skiba MA]] | |||
[[Category: Smith JL]] | |||
[[Category: Tran CL]] | |||
Latest revision as of 06:30, 11 October 2023
GphF GNAT-like decarboxylase in complex with isobutyryl-CoA
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