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'''Unreleased structure'''


The entry 9mc1 is ON HOLD
==Trans-acting enoylreductase PhiaB involved in the phialotideA biosynthesis pathway==
<StructureSection load='9mc1' size='340' side='right'caption='[[9mc1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9mc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudophialophora Pseudophialophora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MC1 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]] 2.9&#8491;</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=9mc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mc1 OCA], [https://pdbe.org/9mc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mc1 RCSB], [https://www.ebi.ac.uk/pdbsum/9mc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mc1 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fungal polyketides are diverse natural products synthesized by iterative polyketide synthases (i-PKSs) and modified by enzymes such as trans-acting enoylreductases (trans-ERs). In this study, we investigated PhiaB and PhomB, trans-ERs involved in the biosynthesis of polyhydroxy polyketides, phialotides, and phomenoic acids. In vitro assays using substrate analogs revealed distinct chain-length preferences. X-ray structural analysis of PhiaB revealed distinct N-terminal, central, and C-terminal regions. The importance of the central region, which possesses a canonical Rossmann fold for cofactor recognition, was further supported by biosynthetic refactoring using a chimeric enzyme. Docking studies revealed key amino acid residues that may be involved in substrate/cofactor recognition. These findings advance our understanding of trans-ER function, providing opportunities for the synthesis of structurally different polyhydroxy polyketides by genetic engineering of polyhydroxy polyketide biosynthesis.


Authors: Takekawa, Y., Takino, J., Sato, S., Yabuno, N., Oikawa, H., Ose, T., Minami, A.
Chain-length preference of trans-acting enoylreductases involved in the biosynthesis of fungal polyhydroxy polyketides.,Takekawa Y, Takino J, Sato S, Oikawa H, Ose T, Minami A Biochem Biophys Res Commun. 2025 May 1;761:151737. doi: , 10.1016/j.bbrc.2025.151737. Epub 2025 Apr 1. PMID:40186921<ref>PMID:40186921</ref>


Description: Trans-acting enoylreductase PhiaB involved in the phialotideA biosynthesis pathway
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Oikawa, H]]
<div class="pdbe-citations 9mc1" style="background-color:#fffaf0;"></div>
[[Category: Minami, A]]
== References ==
[[Category: Takino, J]]
<references/>
[[Category: Takekawa, Y]]
__TOC__
[[Category: Sato, S]]
</StructureSection>
[[Category: Ose, T]]
[[Category: Large Structures]]
[[Category: Yabuno, N]]
[[Category: Pseudophialophora]]
[[Category: Minami A]]
[[Category: Oikawa H]]
[[Category: Ose T]]
[[Category: Sato S]]
[[Category: Takekawa Y]]
[[Category: Takino J]]
[[Category: Yabuno N]]
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