PDBsum entry: 1b0p

Oxidoreductase

PDB-id: 1b0p

Biological unit = asymmetric unit,
as shown
(as defined in PDB file)

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

1231 a.a. *

Ligands

SF4 ×6

TPP ×2

Metal ions

_MG ×2

_CA ×2

Waters ×543

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1b0p

Name:

Oxidoreductase

Title:

Crystal structure of pyruvate-ferredoxin oxidoreductase from desulfovibrio africanus

Structure:

Protein (pyruvate-ferredoxin oxidoreductase). Chain: a, b. Ec: 1.2.7.1

Source:

Desulfovibrio africanus. Organism_taxid: 873. Strain: ncib 8401. Cellular_location: cytoplasm

Biological unit:

Homo-dimer (from PDB file)

UniProt:

Chains A, B: P94692 (P94692_DESAF)

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

Struc:

Seq:

1232 a.a.

Struc:

1231 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

2.31Å

R-factor:

0.199

R-free:

0.271

Authors:

E.Chabriere,M.H.Charon,A.Volbeda

Key ref:

E.Chabrière et al. (1999). Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.. Nat Struct Biol, 6, 182-190. [PubMed id: 10048931] [DOI: 10.1038/5870]

Date:

12-Nov-98

Release date:

23-Apr-99

Quick_links

Procheck

Surface

Key reference

DOI no: 10.1038/5870

Nat Struct Biol 6:182-190 (1999)

PubMed id: 10048931

Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.

E.Chabrière, M.H.Charon, A.Volbeda, L.Pieulle, E.C.Hatchikian, J.C.Fontecilla-Camps.

ABSTRACT

Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial step in many metabolic pathways, is carried out in most aerobic organisms by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design against certain anaerobic pathogens. Here, we report the crystal structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A resolution), and of its complex with pyruvate (3.0 A resolution). The structures show that each subunit consists of seven domains, one of which affords protection against oxygen. The thiamin pyrophosphate (TPP) cofactor and the three [4Fe-4S] clusters are suitably arranged to provide a plausible electron transfer pathway. In addition, the PFOR-pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction.

Selected figure(s)

Figure 1.
Figure 1. Ribbon drawings of Desulfovibrio africanus PFOR, made with MOLSCRIPT^48 and Raster3D^49. a,b, Two perpendicular views. Subunits are shown in light blue and dark blue. TPP cofactors are highlighted in bright red, Mg ions in green, iron atoms in brown and sulfur atoms in yellow.

Figure 3.
Figure 3. Ribbon drawings of the seven structural domains of Desulfovibrio africanus PFOR. In the included topology diagrams, −helices are represented by circles and −strands by triangles. A common folding motif in the core domains I, II and VI is indicated by the dots in their topology diagrams. For clarity, domains and topology diagrams are not represented in the same orientation.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 182-190) copyright 1999.

Figures were selected by an automated process.