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4pu0

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==Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in FMNH2-bound form==
==Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in FMNH2-bound form==
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<StructureSection load='4pu0' size='340' side='right' caption='[[4pu0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4pu0' size='340' side='right'caption='[[4pu0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pu0]] is a 4 chain structure. 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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3018&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pty|4pty]], [[4ptz|4ptz]]</td></tr>
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<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>
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<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>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=4pu0 RCSB], [http://www.ebi.ac.uk/pdbsum/4pu0 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:24816272</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Driggers, C M]]
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[[Category: Escherichia coli K-12]]
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[[Category: Ellis, H R]]
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[[Category: Large Structures]]
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[[Category: Karplus, P A]]
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[[Category: Driggers CM]]
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[[Category: Flavodoxin-like fold]]
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[[Category: Ellis HR]]
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[[Category: Nadph-dependent fmn reductase]]
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[[Category: Karplus PA]]
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[[Category: Oxidoreductase]]
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[[Category: Ssud]]
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Current revision

Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in FMNH2-bound form

PDB ID 4pu0

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