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Crystal structure analysis of Bacillus subtilis ferredoxin‐NADP^+^ oxidoreductase and the structural basis for its substrate selectivity by Hirofumi Komori; Daisuke Seo; Takeshi Sakurai; Yoshiki Higuchi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Crystal structure analysis of Bacillus subtilis ferredoxin‐NADP^+^ oxidoreductase and the structural basis for its substrate selectivity about?

## Abstract __Bacillus subtilis yumC__ encodes a novel type of ferredoxin‐NADP^+^ oxidoreductase (FNR) with a primary sequence and oligomeric conformation distinct from those of previously known FNRs. In this study, the crystal structure of __B. subtilis__ FNR (BsFNR) complexed with NADP^+^ has been determined. BsFNR features two distinct binding domains for FAD and NADPH in accordance with its structural similarity to __Escherichia coli__ NADPH‐thioredoxin reductase (TdR) and TdR‐like protein from __Thermus thermophilus__ HB8 (PDB code: 2ZBW). The deduced mode of NADP^+^ binding to the BsFNR molecule is nonproductive in that the nicotinamide and isoalloxazine rings are over 15 Å apart. A unique C‐terminal extension, not found in __E. coli__ TdR but in TdR‐like protein from __T. thermophilus__ HB8, covers the __re__‐face of the isoalloxazine moiety of FAD. In particular, Tyr50 in the FAD‐binding region and His324 in the C‐terminal extension stack on the __si__‐ and __re‐__faces of the isoalloxazine ring of FAD, respectively. Aromatic residues corresponding to Tyr50 and His324 are also found in the plastid‐type FNR superfamily of enzymes, and the residue corresponding to His324 has

Who reads Crystal structure analysis of Bacillus subtilis ferredoxin‐NADP^+^ oxidoreductase and the structural basis for its substrate selectivity?

Author

Hirofumi Komori; Daisuke Seo; Takeshi Sakurai; Yoshiki Higuchi

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)