21dw: Difference between revisions

Line 1:

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

~~The entry~~ 21dw is ~~ON HOLD until Paper~~ Publication

==Crystal structure of sulX in complex with FMN and sulfamethoxazole==

== Structural highlights ==

<table><tr><td colspan='2'>[[21dw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Microbacterium Unclassified Microbacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=21DW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=21DW 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]] 2.46Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=08D:SULFAMETHOXAZOLE'>08D</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=21dw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=21dw OCA], [https://pdbe.org/21dw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=21dw RCSB], [https://www.ebi.ac.uk/pdbsum/21dw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=21dw ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/A0A482P9Z9_9MICO A0A482P9Z9_9MICO]

== Publication Abstract from PubMed ==

The sulfonamide-degrading monooxygenase sulX plays a dual role in bioremediation and antibiotic resistance, yet its molecular mechanism remains elusive. Here we report crystal structures of sulX in its ligand-free form, as an FMN-bound binary complex, and as ternary complexes with six distinct sulfonamides at resolutions ranging from 2.09 to 3.03â¯A. These structures reveal that sulfonamides bind on the re face of the flavin isoalloxazine ring, with their conserved 4-aminophenol and sulfonyl moieties tightly anchored by pi-stacking and hydrogen-bonding interactions, while the divergent aminated substituents extend into an open cleft with minimal specific contacts-a feature that explains the enzyme's remarkable capacity to accommodate diverse sulfonamide substrates. By integrating structural and biochemical data, we propose a catalytic mechanism involving F265-mediated substrate gating and H397-facilitated proton transfer. In addition, structure-based engineering yielded enhanced variants: A399S, which introduces new hydrogen bonds, showed a 37% increase in activity, and P422K achieved a 29% improvement. Our findings establish the structural basis of sulX-mediated sulfonamide degradation and provide a foundation for understanding sulfonamide resistance mechanisms.

~~Authors~~:

Structural insights into sulfonamide degradation by a two-component flavin-dependent monooxygenase.,Hu Y, Liu W, Zhang Q, Gao Z, Zhang H, Li H, Dai L J Hazard Mater. 2026 Sep 15;517:143643. doi: 10.1016/j.jhazmat.2026.143643. PMID:42748825<ref>PMID:42748825</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: Unclassified Microbacterium]]

[[Category: Dai LH]]

[[Category: Gao ZD]]

[[Category: Hu YM]]

[[Category: Li H]]

[[Category: Liu WH]]

[[Category: Zhang HL]]

[[Category: Zhang QS]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 21dw is ON HOLD  until Paper Publication
+==Crystal structure of sulX in complex with FMN and sulfamethoxazole==
+<StructureSection load='21dw' size='340' side='right'caption='[[21dw]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[21dw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Unclassified_Microbacterium Unclassified Microbacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=21DW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=21DW 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]] 2.46&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=08D:SULFAMETHOXAZOLE'>08D</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=21dw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=21dw OCA], [https://pdbe.org/21dw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=21dw RCSB], [https://www.ebi.ac.uk/pdbsum/21dw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=21dw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A482P9Z9_9MICO A0A482P9Z9_9MICO]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The sulfonamide-degrading monooxygenase sulX plays a dual role in bioremediation and antibiotic resistance, yet its molecular mechanism remains elusive. Here we report crystal structures of sulX in its ligand-free form, as an FMN-bound binary complex, and as ternary complexes with six distinct sulfonamides at resolutions ranging from 2.09 to 3.03â¯A. These structures reveal that sulfonamides bind on the re face of the flavin isoalloxazine ring, with their conserved 4-aminophenol and sulfonyl moieties tightly anchored by pi-stacking and hydrogen-bonding interactions, while the divergent aminated substituents extend into an open cleft with minimal specific contacts-a feature that explains the enzyme's remarkable capacity to accommodate diverse sulfonamide substrates. By integrating structural and biochemical data, we propose a catalytic mechanism involving F265-mediated substrate gating and H397-facilitated proton transfer. In addition, structure-based engineering yielded enhanced variants: A399S, which introduces new hydrogen bonds, showed a 37% increase in activity, and P422K achieved a 29% improvement. Our findings establish the structural basis of sulX-mediated sulfonamide degradation and provide a foundation for understanding sulfonamide resistance mechanisms.
-Authors:
+Structural insights into sulfonamide degradation by a two-component flavin-dependent monooxygenase.,Hu Y, Liu W, Zhang Q, Gao Z, Zhang H, Li H, Dai L J Hazard Mater. 2026 Sep 15;517:143643. doi: 10.1016/j.jhazmat.2026.143643. PMID:42748825<ref>PMID:42748825</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 21dw" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Unclassified Microbacterium]]
+[[Category: Dai LH]]
+[[Category: Gao ZD]]
+[[Category: Hu YM]]
+[[Category: Li H]]
+[[Category: Liu WH]]
+[[Category: Zhang HL]]
+[[Category: Zhang QS]]