PDBsum entry 1fdr

Flavoprotein

PDB id: 1fdr

Contents

Protein chain

244 a.a. *

Ligands

FAD

Waters ×205

* Residue conservation analysis

PDB id:

1fdr

Name:

Flavoprotein

Title:

Flavodoxin reductase from e. Coli

Structure:

Flavodoxin reductase. Chain: a. Synonym: ferredoxin reductase. Engineered: yes. Mutation: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: k12 c600. Cellular_location: cytoplasm. Gene: fpr. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.70Å R-factor: 0.184 R-free: 0.248

Authors:

M.Ingelman,V.Bianchi,H.Eklund

Key ref:

M.Ingelman et al. (1997). The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution. J Mol Biol, 268, 147-157. PubMed id: 9149148 DOI: 10.1006/jmbi.1997.0957

Date:

06-Mar-97 Release date: 17-Sep-97

Protein chain

P28861  (FENR_ECOLI) -  Flavodoxin/ferredoxin--NADP reductase from Escherichia coli (strain K12)

Seq: 248 a.a.

Struc: 244 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 2: E.C.1.18.1.2 - ferredoxin--NADP(+) reductase.
• Pathway: Methionine Synthase
• Reaction: 2 reduced [2Fe-2S]-[ferredoxin] + NADP⁺ + H⁺ = 2 oxidized [2Fe-2S]- [ferredoxin] + NADPH
• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

• Enzyme class 3: E.C.1.19.1.1 - flavodoxin--NADP(+) reductase.
• Reaction: reduced [flavodoxin] + NADP⁺ = oxidized [flavodoxin] + NADPH + 2 H⁺
• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1006/jmbi.1997.0957

J Mol Biol 268:147-157 (1997)

PubMed id: 9149148

The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution.

M.Ingelman, V.Bianchi, H.Eklund.

ABSTRACT

Flavodoxin reductase from Escherichia coli is an FAD-containing oxidoreductase that transports electrons between flavodoxin or ferredoxin and NADPH. Together with flavodoxin, the enzyme is involved in the reductive activation of three E. coli enzymes: cobalamin-dependent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. An additional function for the oxidoreductase appears to be to protect the bacteria against oxygen radicals. The three-dimensional structure of flavodoxin reductase has been solved by multiple isomorphous replacement, and has been refined at 1.7 A to an R-value of 18.4% and Rfree 24.8%. The monomeric molecule contains one beta-sandwich FAD domain and an alpha/beta NADP domain. The overall structure is similar to other reductases of the NADP-ferredoxin reductase family in spite of the low sequence similarities within the family. Flavodoxin reductase lacks the loop which is involved in the binding of the adenosine moiety of FAD in other FAD binding enzymes of the superfamily but is missing in the FMN binding phthalate dioxygenase reductase. Instead of this loop, the adenine interacts with an extra tryptophan at the C terminus. The FAD in flavodoxin reductase has an unusual bent conformation with a hydrogen bond between the adenine and the isoalloxazine. This is probably the cause of the unusual spectrum of the enzyme. There is a pronounced cleft close to the isoalloxazine that appears to be well suited for binding of flavodoxin/ferredoxin. Two extra short strands of the NADP-binding domain probably act as an anchor point for the binding of flavodoxin.

Selected figure(s)

Figure 2.
Figure 2. Ribbon representation of the flavodoxin reductase molecule made with the program MOLSCRIPT [Kraulis 1991]. The secondary structure elements are labelled essentially as by [Correll et al 1993]. Fβ1, 3–16; Fβ2, 17–26; Fβ3, 35–41; Fβ4, 48–54; Fβ5, 63–69; Fα1, 75–82; Fβ6, 85–92; 3[10], 99–103; Nβ1, 107–114; Nα1, 118–128; 3[10], 131–134; Nβ2, 135–144; Nα2, 151–163; Nβ3, 165–174; Nβ4, 181–183; Nα3a, 184–192; Nα3b, 192–200; Nβ5, 206–213; Nα4, 214–230; βA, 232–236; βB, 237–241; Nβ6, 241–247. The FAD molecule is included as a ball-and-stick model.

Figure 7.
Figure 7. Stereo view surface representation of the flavodoxin reductase made with the program GRASP [Nicholls et al 1993]. Positive potential is shown in blue and negative potential in red. The FAD molecule is indicated in the middle.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1997, 268, 147-157) copyright 1997.

Figures were selected by an automated process.