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| | <StructureSection load='4pu0' size='340' side='right'caption='[[4pu0]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4pu0' size='340' side='right'caption='[[4pu0]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pu0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PU0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pu0]] is a 4 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=4PU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PU0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pty|4pty]], [[4ptz|4ptz]]</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=4pu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pu0 OCA], [https://pdbe.org/4pu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pu0 RCSB], [https://www.ebi.ac.uk/pdbsum/4pu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pu0 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ssuE, ycbP, b0937, JW0920 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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='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=4pu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pu0 OCA], [http://pdbe.org/4pu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pu0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pu0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pu0 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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Driggers, C M]] | + | [[Category: Driggers CM]] |
| - | [[Category: Ellis, H R]] | + | [[Category: Ellis HR]] |
| - | [[Category: Karplus, P A]] | + | [[Category: Karplus PA]] |
| - | [[Category: Flavodoxin-like fold]]
| + | |
| - | [[Category: Nadph-dependent fmn reductase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Ssud]]
| + | |
| 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 Escherichia coli sulfur starvation utilization (ssu) operon includes a two-component monooxygenase system consisting of a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent flavin mononucleotide (FMN) reductase, SsuE, and a monooxygenase, SsuD. SsuE is part of the flavodoxin-like superfamily, and we report here the crystal structures of its apo, FMN-bound, and FMNH2-bound forms at approximately 2 A resolution. In the crystals, SsuE forms a tetramer that is a dimer of dimers similar to those seen for homologous FMN reductases, quinone reductases, and the WrbA family of enzymes. A pi-helix present at the tetramer building interface is unique to the reductases from two-component monooxygenase systems. Analytical ultracentrifugation studies of SsuE confirm a dimer-tetramer equilibrium exists in solution, with FMN binding favoring the dimer. As the active site includes residues from both subunits, at least a dimeric association is required for the function of SsuE. The structures show that one FMN binds tightly in a deeply held site, which makes available a second binding site, in which either a second FMN or the nicotinamide of NADPH can bind. The FMNH2-bound structure shows subtle changes consistent with its binding being weaker than that of FMN. Combining this information with published kinetic studies, we propose a general catalytic cycle for two-component reductases of the flavodoxin-like superfamily, by which the enzyme can potentially provide FMNH2 to its partner monooxygenase by different routes depending on the FMN concentration and the presence of a partner monooxygenase.
Crystal Structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN Reductases of the Flavodoxin-like Superfamily.,Driggers CM, Dayal PV, Ellis HR, Karplus PA Biochemistry. 2014 Jun 3;53(21):3509-19. doi: 10.1021/bi500314f. Epub 2014 May, 21. PMID:24816272[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Driggers CM, Dayal PV, Ellis HR, Karplus PA. Crystal Structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN Reductases of the Flavodoxin-like Superfamily. Biochemistry. 2014 Jun 3;53(21):3509-19. doi: 10.1021/bi500314f. Epub 2014 May, 21. PMID:24816272 doi:http://dx.doi.org/10.1021/bi500314f
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