|
|
| Line 3: |
Line 3: |
| | <StructureSection load='7jw9' size='340' side='right'caption='[[7jw9]], [[Resolution|resolution]] 2.39Å' scene=''> | | <StructureSection load='7jw9' size='340' side='right'caption='[[7jw9]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7jw9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Psepf Psepf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JW9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7jw9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens_Pf0-1 Pseudomonas fluorescens Pf0-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JW9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=03S:METHANESULFONIC+ACID'>03S</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.39Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msuD, ssuD, Pfl01_3916 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=205922 PSEPF])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=03S:METHANESULFONIC+ACID'>03S</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alkanesulfonate_monooxygenase Alkanesulfonate monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.5 1.14.14.5] </span></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=7jw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jw9 OCA], [https://pdbe.org/7jw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jw9 RCSB], [https://www.ebi.ac.uk/pdbsum/7jw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jw9 ProSAT]</span></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=7jw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jw9 OCA], [https://pdbe.org/7jw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jw9 RCSB], [https://www.ebi.ac.uk/pdbsum/7jw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jw9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q3K9A1_PSEPF Q3K9A1_PSEPF]] Catalyzes the desulfonation of aliphatic sulfonates.[HAMAP-Rule:MF_01229]
| + | [https://www.uniprot.org/uniprot/Q3K9A1_PSEPF Q3K9A1_PSEPF] Catalyzes the desulfonation of aliphatic sulfonates.[HAMAP-Rule:MF_01229] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alkanesulfonate monooxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Psepf]] | + | [[Category: Pseudomonas fluorescens Pf0-1]] |
| - | [[Category: Dowling, D P]] | + | [[Category: Dowling DP]] |
| - | [[Category: Liew, J J.M]] | + | [[Category: Liew JJM]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q3K9A1_PSEPF Catalyzes the desulfonation of aliphatic sulfonates.[HAMAP-Rule:MF_01229]
Publication Abstract from PubMed
Bacterial two-component flavin-dependent monooxygenases cleave the stable C-S bond of environmental and anthropogenic organosulfur compounds. The monooxygenase MsuD converts methanesulfonate (MS(-)) to sulfite, completing the sulfur assimilation process during sulfate starvation, but the mechanism of this conversion remains unclear. To explore the mechanism of C-S bond cleavage, we report a series of crystal structures of MsuD from Pseudomonas fluorescens in different liganded states. This report provides the first crystal structures of an alkanesulfonate monooxygenase with a bound flavin and alkanesulfonate, elucidating the roles of the active site lid, the protein C-terminus, and an active site loop in flavin and/or alkanesulfonate binding. These structures position MS(-) closest to the flavin N5 position, consistent with an N5-(hydro)peroxyflavin mechanism rather than a classical C4a-(hydro)peroxyflavin mechanism. A fully enclosed active site is observed in the ternary complex, mediated by interchain interaction of the C-terminus at the tetramer interface. These structures identify an unexpected function of the protein C-terminus in this protein family in stabilizing tetramer formation and the alkanesulfonate binding site. Spurred by interest from the crystal structures, we conducted biochemical assays and molecular docking that redefine MsuD as a small to medium chain alkanesulfonate monooxygenase. Functional mutations verify the sulfonate binding site and reveal the critical importance of the protein C-terminus for monooxygenase function. These findings reveal a deeper understanding of MsuD's functionality at the molecular level, and consequently how it operates within its role as part of the sulfur assimilation pathway.
Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer.,Liew JJM, El Saudi I, Nguyen SV, Wicht DK, Dowling DP J Biol Chem. 2021 May 21:100823. doi: 10.1016/j.jbc.2021.100823. PMID:34029591[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liew JJM, El Saudi I, Nguyen SV, Wicht DK, Dowling DP. Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer. J Biol Chem. 2021 May 21:100823. doi: 10.1016/j.jbc.2021.100823. PMID:34029591 doi:http://dx.doi.org/10.1016/j.jbc.2021.100823
|
