"7"^^ . "Protein WrbA tvo\u0159\u00ED most mezi bakterialn\u00EDmi Flavodoxiny a eukariotn\u00EDmi NAD(P)H zavisl\u00FDmi chinon oxidoreduktasami"@cs . "Grandori, R." . . "461426" . "The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1." . "Kut\u00E1-Smatanov\u00E1, Ivana" . "Ettrich, R\u00FCdiger" . "0961-8368" . "[BF54D3647B58]" . "1"^^ . "Gustavsson, T." . . . . "WrbA bridges bacterial flavonoids and eukaryotic NAD(P)H:quinone oxidoreductases"@en . . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "Krystalov\u00E1 struktura flavodoxinu podobn\u00E9ho proteinu WrbA s nav\u00E1zan\u00FDm FMN odhaluje bl\u00EDzkou struturn\u00ED p\u0159\u00EDbuznost s eukariotn\u00EDmi NAD(P)H zavisl\u00FDmi chinon oxidoreduktasami, Nqo1. Porovn\u00E1n\u00ED krystalov\u00FDch struktur WrbA, Flavodoxinu a Nqo1 ukazuje jak je sto\u010Den\u00E1 otev\u0159en\u00E1 struktura beta skl\u00E1dan\u00E9ho listu uspo\u0159\u00E1d\u00E1na tak, aby vznikl multimer, kter\u00FD roz\u0161i\u0159uje katalitickou funkci z jednoelektronov\u00E9ho p\u0159enosu na dvouelektronov\u00FD. Strukturn\u00ED anal\u00FDza nazna\u010Duje mo\u017En\u00E9 nov\u00E9 fyziologick\u00E9 funkce protein\u016F WrbA a Nqo1."@cs . . "Z(AV0Z50520514), Z(AV0Z60870520)" . "16" . "5"^^ . "RIV/68378050:_____/07:00097983!RIV08-AV0-68378050" . "Protein Science" . . "10" . . . . . "The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1."@en . "Brynda, Ji\u0159\u00ED" . "WrbA bridges bacterial flavonoids and eukaryotic NAD(P)H:quinone oxidoreductases" . . . "Carey, J." . "Protein WrbA tvo\u0159\u00ED most mezi bakterialn\u00EDmi Flavodoxiny a eukariotn\u00EDmi NAD(P)H zavisl\u00FDmi chinon oxidoreduktasami"@cs . . "RIV/68378050:_____/07:00097983" . . "Wolfov\u00E1, Julie" . "WrbA bridges bacterial flavonoids and eukaryotic NAD(P)H:quinone oxidoreductases" . "WrbA bridges bacterial flavonoids and eukaryotic NAD(P)H:quinone oxidoreductases"@en . . "WrbA; crystal structure; Nqo1; oxidoreductases"@en . . "2301;2305" .