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| | ==Crystal structure of SsuE FMN reductase Delta118 mutant in apo form== | | ==Crystal structure of SsuE FMN reductase Delta118 mutant in apo form== |
| - | <StructureSection load='6dqp' size='340' side='right' caption='[[6dqp]], [[Resolution|resolution]] 1.55Å' scene=''> | + | <StructureSection load='6dqp' size='340' side='right'caption='[[6dqp]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dqp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DQP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dqp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DQP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.546Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6dqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqp OCA], [http://pdbe.org/6dqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dqp RCSB], [http://www.ebi.ac.uk/pdbsum/6dqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqp 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=6dqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqp OCA], [https://pdbe.org/6dqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dqp RCSB], [https://www.ebi.ac.uk/pdbsum/6dqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI]] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin. | + | [https://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ellis, H R]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Lamb, A L]] | + | [[Category: Large Structures]] |
| - | [[Category: McFarlane, J S]] | + | [[Category: Ellis HR]] |
| - | [[Category: Flavoprotein]] | + | [[Category: Lamb AL]] |
| - | [[Category: Fmn]] | + | [[Category: McFarlane JS]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| Structural highlights
Function
SSUE_ECOLI Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
Publication Abstract from PubMed
The pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the pi-helix. The structure of the Y118A SsuE pi-helix was converted to an alpha-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the pi-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the pi-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Delta118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the pi-helix contains a His insertional residue. Exchanging the pi-helix insertional residue of each enzyme did not result in equivalent kinetic properties. Structure-based sequence analysis further demonstrated the presence of a similar Tyr residue in an FMN-bound reductase in the NADPH:FMN reductase family that is not sufficient to generate a pi-helix. Results from the structural and functional studies of the FMN-dependent reductases suggest that the insertional residue alone is not solely responsible for generating the pi-helix, and additional structural adaptions occur to provide the altered gain of function.
Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.,McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR. Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases. Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650 doi:http://dx.doi.org/10.1002/pro.3504
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