View source for 6mfd


==GphF GNAT-like decarboxylase in complex with isobutyryl-CoA==
<StructureSection load='6mfd' size='340' side='right'caption='[[6mfd]], [[Resolution|resolution]] 2.79&Aring;' 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]] 2.794&#8491;</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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]]