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| | <StructureSection load='6mfc' size='340' side='right'caption='[[6mfc]], [[Resolution|resolution]] 2.59Å' scene=''> | | <StructureSection load='6mfc' size='340' side='right'caption='[[6mfc]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"archangium_violaceum"_kuhlwein_and_reichenbach_1964 "archangium violaceum" kuhlwein and reichenbach 1964]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mfc]] 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=6MFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MFC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.589Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gphF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83451 "Archangium violaceum" Kuhlwein and Reichenbach 1964])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfc OCA], [http://pdbe.org/6mfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mfc RCSB], [http://www.ebi.ac.uk/pdbsum/6mfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfc 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=6mfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mfc OCA], [https://pdbe.org/6mfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mfc RCSB], [https://www.ebi.ac.uk/pdbsum/6mfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mfc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/U6BSB2_9DELT U6BSB2_9DELT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Archangium violaceum kuhlwein and reichenbach 1964]] | + | [[Category: Archangium violaceum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Skiba, M A]] | + | [[Category: Skiba MA]] |
| - | [[Category: Smith, J L]] | + | [[Category: Smith JL]] |
| - | [[Category: Tran, C L]] | + | [[Category: Tran CL]] |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
U6BSB2_9DELT
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Skiba MA, Tran CL, Dan Q, Sikkema AP, Klaver Z, Gerwick WH, Sherman DH, Smith JL. Repurposing the GNAT Fold in the Initiation of Polyketide Biosynthesis. Structure. 2020 Jan 7;28(1):63-74.e4. doi: 10.1016/j.str.2019.11.004. Epub 2019, Nov 27. PMID:31785925 doi:http://dx.doi.org/10.1016/j.str.2019.11.004
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