1gr1
STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH GLU 139 REPLACED BY LYS (E139K)
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OverviewOverview
The role of the negative charge of the E139 side-chain of Anabaena, Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its, substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient, electron transfer (ET) is analysed by characterization of several E139 FNR, mutants. Replacement of E139 affects the interaction with the different, FNR substrates in very different ways. Thus, while E139 does not appear to, be involved in the processes of binding and ET between FNR and NADP+/H, the nature and the conformation of the residue at position 139 of Anabaena, FNR modulates the precise enzyme interaction with the protein carriers, ferredoxin (Fd) and flavodoxin (Fld). Introduction of the shorter aspartic, acid side-chain at position 139 produces an enzyme that ... [(full description)]
About this StructureAbout this Structure
1GR1 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: FAD. Full crystallographic information is available from [OCA].
ReferenceReference
Probing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substrates., Faro M, Frago S, Mayoral T, Hermoso JA, Sanz-Aparicio J, Gomez-Moreno C, Medina M, Eur J Biochem. 2002 Oct;269(20):4938-47. PMID:12383252
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