6b39

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==AprA Methyltransferase 1 - GNAT in complex with SAH==
==AprA Methyltransferase 1 - GNAT in complex with SAH==
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<StructureSection load='6b39' size='340' side='right' caption='[[6b39]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
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<StructureSection load='6b39' size='340' side='right'caption='[[6b39]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6b39]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B39 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6b39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorena_bouillonii Moorena bouillonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B39 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.392&#8491;</td></tr>
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<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=6b39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b39 OCA], [http://pdbe.org/6b39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b39 RCSB], [http://www.ebi.ac.uk/pdbsum/6b39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b39 ProSAT]</span></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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6b39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b39 OCA], [https://pdbe.org/6b39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b39 RCSB], [https://www.ebi.ac.uk/pdbsum/6b39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b39 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1U7N2Z8_9CYAN A0A1U7N2Z8_9CYAN]
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Natural product biosynthetic pathways contain a plethora of enzymatic tools to carry out difficult biosynthetic transformations. Here, we discover an unusual mononuclear iron-dependent methyltransferase that acts in the initiation steps of apratoxin A biosynthesis (AprA MT1). Fe3+-replete AprA MT1 catalyzes one or two methyl transfer reactions on the substrate malonyl-ACP (acyl carrier protein), whereas Co2+, Fe2+, Mn2+, and Ni2+ support only a single methyl transfer. MT1 homologues exist within the "GNAT" (GCN5-related N-acetyltransferase) loading modules of several modular biosynthetic pathways with propionyl, isobutyryl, or pivaloyl starter units. GNAT domains are thought to catalyze decarboxylation of malonyl-CoA and acetyl transfer to a carrier protein. In AprA, the GNAT domain lacks both decarboxylation and acyl transfer activity. A crystal structure of the AprA MT1-GNAT di-domain with bound Mn2+, malonate, and the methyl donor S-adenosylmethionine (SAM) reveals that the malonyl substrate is a bidentate metal ligand, indicating that the metal acts as a Lewis acid to promote methylation of the malonyl alpha-carbon. The GNAT domain is truncated relative to functional homologues. These results afford an expanded understanding of MT1-GNAT structure and activity and permit the functional annotation of homologous GNAT loading modules both with and without methyltransferases, additionally revealing their rapid evolutionary adaptation in different biosynthetic contexts.
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A Mononuclear Iron-Dependent Methyltransferase Catalyzes Initial Steps in Assembly of the Apratoxin A Polyketide Starter Unit.,Skiba MA, Sikkema AP, Moss NA, Tran CL, Sturgis RM, Gerwick L, Gerwick WH, Sherman DH, Smith JL ACS Chem Biol. 2017 Nov 14. doi: 10.1021/acschembio.7b00746. PMID:29096064<ref>PMID:29096064</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6b39" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Skiba, M A]]
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[[Category: Large Structures]]
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[[Category: Smith, J L]]
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[[Category: Moorena bouillonii]]
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[[Category: Apratoxin]]
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[[Category: Skiba MA]]
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[[Category: Gcn5 related n-acetyltransferase]]
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[[Category: Smith JL]]
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[[Category: Methyltransferase]]
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[[Category: Transferase]]
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Current revision

AprA Methyltransferase 1 - GNAT in complex with SAH

PDB ID 6b39

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