1I0R

CRYSTAL STRUCTURE OF FERRIC REDUCTASE FROM ARCHAEOGLOBUS FULGIDUS

Summary for 1I0R

• Entry DOI: 10.2210/pdb1i0r/pdb
• Related: 1I0S 1flm 1qfj 1qfy
• Descriptor: CONSERVED HYPOTHETICAL PROTEIN, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: six stranded antiparallel beta-barrel, fmn and nadp+ binding domain, oxidoreductase
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 2
• Total formula weight: 37822.90

Authors

Chiu, H.-J.,Johnson, E.,Schroder, I.,Rees, D.C. (deposition date: 2001-01-29, release date: 2001-05-02, Last modification date: 2024-10-16)

Primary citation

Chiu, H.J.,Johnson, E.,Schroder, I.,Rees, D.C.
Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+.
Structure, 9:311-319, 2001

PubMed Abstract: Studies performed within the last decade have indicated that microbial reduction of Fe(III) to Fe(II) is a biologically significant process. The ferric reductase (FeR) from Archaeoglobus fulgidus is the first reported archaeal ferric reductase and it catalyzes the flavin-mediated reduction of ferric iron complexes using NAD(P)H as the electron donor. Based on its catalytic activity, the A. fulgidus FeR resembles the bacterial and eukaryotic assimilatory type of ferric reductases. However, the high cellular abundance of the A. fulgidus FeR (approximately 0.75% of the total soluble protein) suggests a catabolic role for this enzyme as the terminal electron acceptor in a ferric iron-based respiratory pathway [1].

PubMed: 11525168
DOI: 10.1016/S0969-2126(01)00589-5

Experimental method

X-RAY DIFFRACTION (1.5 Å)