| http://purl.uniprot.org/citations/24816272 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24816272 | http://www.w3.org/2000/01/rdf-schema#comment | "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 ∼2 Å 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 π-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."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi500314f"xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/author | "Karplus P.A."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/author | "Ellis H.R."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/author | "Driggers C.M."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/author | "Dayal P.V."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/pages | "3509-3519"xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/title | "Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily."xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://purl.uniprot.org/core/volume | "53"xsd:string |
| http://purl.uniprot.org/citations/24816272 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/24816272 |
| http://purl.uniprot.org/citations/24816272 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/24816272 |
| http://purl.uniprot.org/uniprot/#_P80644-mappedCitation-24816272 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/24816272 |
| http://purl.uniprot.org/uniprot/P80644 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/24816272 |