9l10: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 9l10 is ~~ON HOLD~~

==Crystal structure of flavin reductase (StnC) complexed with FMN==

== Structural highlights ==

<table><tr><td colspan='2'>[[9l10]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9L10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9L10 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]] 2.61Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=9l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9l10 OCA], [https://pdbe.org/9l10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9l10 RCSB], [https://www.ebi.ac.uk/pdbsum/9l10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9l10 ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/L7PH54_9ACTN L7PH54_9ACTN] Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.[HAMAP-Rule:MF_01216] Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.[HAMAP-Rule:MF_01216]

== Publication Abstract from PubMed ==

The reductase components of two-component flavoprotein monooxygenases (FPMOs) can reduce flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) for their monooxygenase partners. Typically, the type of flavin cofactor bound by a flavoenzyme dictates the cofactor applied in its catalytic reactions. Here, we report the discovery of StnC, a previously unknown reductase family member involved in the biosynthesis of streptonigrin, a potent antimicrobial and antitumor compound. StnC exhibits a paradoxical performance in binding ability and catalytic activity toward flavins. Specifically, it binds FMN 147-fold stronger than FAD, but reduces FAD six times faster than FMN, enabling it to supply reduced FAD to its FAD-preferred monooxygenase partner StnD efficiently. Crystallographic, computational, and structural comparative analyses identified key residues and distinct structural features in StnC-like reductases, including extended clamp-like loops, that enable tight FMN binding and efficient FAD reduction. These features define a family of FAD-preferred reductases under physiological conditions. Our findings significantly broaden the understanding of the sequence-structure-function relationships in FPMO reductase components, uncover a structurally unique family of FAD-preferred reductases, and provide mechanistic insights into their coordination with monooxygenase partners.

~~Authors~~:

A new family of StnC-like pseudo-FMN-preferred reductase components in two-component flavoprotein monooxygenases.,Xie X, Wang X, Yang X, Ji S, Ouyang X, Zhou Z, Xiao Z, Guo W, Liang R, Huang T, Deng Z, Zhao YL, Lin S Int J Biol Macromol. 2025 Sep 9;328(Pt 2):147543. doi: , 10.1016/j.ijbiomac.2025.147543. PMID:40935041<ref>PMID:40935041</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Streptomyces albus]]

[[Category: Lin S]]

[[Category: Xie X]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 9l10 is ON HOLD
+==Crystal structure of flavin reductase (StnC) complexed with FMN==
+<StructureSection load='9l10' size='340' side='right'caption='[[9l10]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[9l10]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9L10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9L10 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]] 2.61&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=9l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9l10 OCA], [https://pdbe.org/9l10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9l10 RCSB], [https://www.ebi.ac.uk/pdbsum/9l10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9l10 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/L7PH54_9ACTN L7PH54_9ACTN] Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.[HAMAP-Rule:MF_01216]  Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.[HAMAP-Rule:MF_01216]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The reductase components of two-component flavoprotein monooxygenases (FPMOs) can reduce flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) for their monooxygenase partners. Typically, the type of flavin cofactor bound by a flavoenzyme dictates the cofactor applied in its catalytic reactions. Here, we report the discovery of StnC, a previously unknown reductase family member involved in the biosynthesis of streptonigrin, a potent antimicrobial and antitumor compound. StnC exhibits a paradoxical performance in binding ability and catalytic activity toward flavins. Specifically, it binds FMN 147-fold stronger than FAD, but reduces FAD six times faster than FMN, enabling it to supply reduced FAD to its FAD-preferred monooxygenase partner StnD efficiently. Crystallographic, computational, and structural comparative analyses identified key residues and distinct structural features in StnC-like reductases, including extended clamp-like loops, that enable tight FMN binding and efficient FAD reduction. These features define a family of FAD-preferred reductases under physiological conditions. Our findings significantly broaden the understanding of the sequence-structure-function relationships in FPMO reductase components, uncover a structurally unique family of FAD-preferred reductases, and provide mechanistic insights into their coordination with monooxygenase partners.
-Authors:
+A new family of StnC-like pseudo-FMN-preferred reductase components in two-component flavoprotein monooxygenases.,Xie X, Wang X, Yang X, Ji S, Ouyang X, Zhou Z, Xiao Z, Guo W, Liang R, Huang T, Deng Z, Zhao YL, Lin S Int J Biol Macromol. 2025 Sep 9;328(Pt 2):147543. doi: , 10.1016/j.ijbiomac.2025.147543. PMID:40935041<ref>PMID:40935041</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 9l10" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptomyces albus]]
+[[Category: Lin S]]
+[[Category: Xie X]]