1w35
FERREDOXIN-NADP+ REDUCTASE (MUTATION: Y 303 W)
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OverviewOverview
Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH, in an overall reversible reaction, showing some differences in the, mechanisms between cyanobacterial and higher plant FNRs. During hydride, transfer it is proposed that the FNR C-terminal Tyr is displaced by the, nicotinamide. Thus, this C-terminal Tyr might be involved not only in, modulating the flavin redox properties, as already shown, but also in, nicotinamide binding and hydride transfer. FNR variants from the, cyanobacterium Anabaena in which the C-terminal Tyr has been replaced by, Trp, Phe, or Ser have been produced. All FNR variants show enhanced NADP+, and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable, improvement of NADH-dependent reactions. Nevertheless, the Tyr303Ser, ... [(full description)]
About this StructureAbout this Structure
1W35 is a [Single protein] structure of sequence from [Anabaena sp.] with SO4 and FAD as [ligands]. Active as [Ferredoxin--NADP(+) reductase], with EC number [1.18.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H., Tejero J, Perez-Dorado I, Maya C, Martinez-Julvez M, Sanz-Aparicio J, Gomez-Moreno C, Hermoso JA, Medina M, Biochemistry. 2005 Oct 18;44(41):13477-90. PMID:16216071
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