9ry8: Difference between revisions
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==Crystal structure of PfaB from Shewanella baltica strain 6-42== | |||
<StructureSection load='9ry8' size='340' side='right'caption='[[9ry8]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9ry8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_baltica Shewanella baltica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RY8 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]] 2.9Å</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=9ry8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ry8 OCA], [https://pdbe.org/9ry8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ry8 RCSB], [https://www.ebi.ac.uk/pdbsum/9ry8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ry8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Omega-3 polyunsaturated fatty acids (PUFAs) are essential for human health due to their numerous beneficial biological properties. These compounds are synthesized in marine bacteria and eukaryotic microalgae by PUFA megasynthases (Pfas), which are evolutionarily related to fatty acid synthases (FAS) and polyketide synthases (PKS). In FAS, PKS, and PUFA synthases, the acyltransferase (AT) domain plays a critical role in condensation reactions by loading starter or extender units into the acyl carrier protein (ACP) domain. PfaB, a component of PUFA megasynthases, harbors a pseudo-ketosynthase (KS') domain and an AT domain. In this study, we show that PfaB determines the final PUFA product, as demonstrated by in vivo assays in Escherichia coli using the DHA-producing Moritella marina and the EPA-producing Shewanella baltica. In vitro biochemical assays confirm that PfaB exhibits acyltransferase activity, with distinct substrate specificity from the AT domain of PfaA. Finally, we report the crystal structure of PfaB from S. baltica, representing the first structurally resolved AT domain within a PUFA megasynthase. Molecular docking analyses suggest that specific residues may contribute to differences in substrate recognition and specificity. Together, these findings show that PfaB acts as the terminal acyltransferase, providing new insights into its functional role in PUFA biosynthesis, and advancing our understanding of its mechanism and ligand interactions. | |||
Prokaryotic PfaB is a terminal acyltransferase that determines the final PUFA product.,Lofeudo N, Martin A, Jacome M, Wan X, Lucas M, Moncalian G Protein Sci. 2026 Mar;35(3):e70497. doi: 10.1002/pro.70497. PMID:41676921<ref>PMID:41676921</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9ry8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shewanella baltica]] | |||
[[Category: Jacome M]] | |||
[[Category: Lofeudo N]] | |||
[[Category: Lucas M]] | |||
[[Category: Martin A]] | |||
[[Category: Moncalian G]] | |||
[[Category: Wan X]] | |||
