PDBsum entry 2rc5

Oxidoreductase

PDB id: 2rc5

Contents

Protein chains

306 a.a. *

Ligands

SO4 ×7

FAD ×4

Metals

_ZN

Waters ×1238

* Residue conservation analysis

PDB id:

2rc5

Name:

Oxidoreductase

Title:

Refined structure of fnr from leptospira interrogans

Structure:

Ferredoxin-NADP reductase. Chain: a, b, c, d. Engineered: yes

Source:

Leptospira interrogans. Organism_taxid: 173. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.43Å R-factor: 0.225 R-free: 0.255

Authors:

A.S.Nascimento,D.L.Catalano-Dupuy,I.Polikarpov,E.A.Ceccarelli

Key ref:

A.S.Nascimento et al. (2007). Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+. Bmc Struct Biol, 7, 69. PubMed id: 17958910

Date:

19-Sep-07 Release date: 25-Mar-08

Protein chains

Q8EY89  (Q8EY89_LEPIN) -  Ferredoxin--NADP reductase from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)

Seq: 310 a.a.

Struc: 306 a.a.

Enzyme reactions

• Enzyme class: 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)

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

reference

Bmc Struct Biol 7:69 (2007)

PubMed id: 17958910

Crystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+.

A.S.Nascimento, D.L.Catalano-Dupuy, A.Bernardes, M.d.e. .O.Neto, M.A.Santos, E.A.Ceccarelli, I.Polikarpov.

ABSTRACT

BACKGROUND: Ferredoxin-NADP(H) reductases (FNRs) are flavoenzymes that catalyze the electron transfer between NADP(H) and the proteins ferredoxin or flavodoxin. A number of structural features distinguish plant and bacterial FNRs, one of which is the mode of the cofactor FAD binding. Leptospira interrogans is a spirochaete parasitic bacterium capable of infecting humans and mammals in general. Leptospira interrogans FNR (LepFNR) displays low sequence identity with plant (34% with Zea mays) and bacterial (31% with Escherichia coli) FNRs. However, LepFNR contains all consensus sequences that define the plastidic class FNRs. RESULTS: The crystal structures of the FAD-containing LepFNR and the complex of the enzyme with NADP+, were solved and compared to known FNRs. The comparison reveals significant structural similarities of the enzyme with the plastidic type FNRs and differences with the bacterial enzymes. Our small angle X-ray scattering experiments show that LepFNR is a monomeric enzyme. Moreover, our biochemical data demonstrate that the LepFNR has an enzymatic activity similar to those reported for the plastidic enzymes and that is significantly different from bacterial flavoenzymes, which display lower turnover rates. CONCLUSION: LepFNR is the first plastidic type FNR found in bacteria and, despite of its low sequence similarity with plastidic FNRs still displays high catalytic turnover rates. The typical structural and biochemical characteristics of plant FNRs unveiled for LepFNR support a notion of a putative lateral gene transfer which presumably offers Leptospira interrogans evolutionary advantages. The wealth of structural information about LepFNR provides a molecular basis for advanced drugs developments against leptospirosis.