This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


6b39

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:19, 13 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==AprA Methyltransferase 1 - GNAT in complex with SAH==
==AprA Methyltransferase 1 - GNAT in complex with SAH==
-
<StructureSection load='6b39' size='340' side='right' caption='[[6b39]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
+
<StructureSection load='6b39' size='340' side='right'caption='[[6b39]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<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>
+
<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>
-
</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>
+
</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>
-
<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>
+
<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>
 +
<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>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A1U7N2Z8_9CYAN A0A1U7N2Z8_9CYAN]
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6b39" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Skiba, M A]]
+
[[Category: Large Structures]]
-
[[Category: Smith, J L]]
+
[[Category: Moorena bouillonii]]
-
[[Category: Apratoxin]]
+
[[Category: Skiba MA]]
-
[[Category: Gcn5 related n-acetyltransferase]]
+
[[Category: Smith JL]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Transferase]]
+

Current revision

AprA Methyltransferase 1 - GNAT in complex with SAH

PDB ID 6b39

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools