PDBsum entry 2vim

Oxidoreductase

PDB id: 2vim

Contents

Protein chain

104 a.a. *

Waters ×103

* Residue conservation analysis

PDB id:

2vim

Name:

Oxidoreductase

Title:

X-ray structure of fasciola hepatica thioredoxin

Structure:

Thioredoxin. Chain: a. Synonym: trx. Engineered: yes

Source:

Fasciola hepatica. Liver fluke. Organism_taxid: 6192. Expressed in: escherichia coli. Expression_system_taxid: 511693.

Resolution:

1.38Å R-factor: 0.192 R-free: 0.248

Authors:

K.Line,M.N.Isupov,E.Garcia-Rodriguez,G.Maggioli,F.Parra, J.A.Littlechild

Key ref:

K.Line et al. (2008). The Fasciola hepatica thioredoxin: High resolution structure reveals two oxidation states. Mol Biochem Parasitol, 161, 44-48. PubMed id: 18620002 DOI: 10.1016/j.molbiopara.2008.06.009

Date:

05-Dec-07 Release date: 29-Jul-08

Protein chain

Q9U1G7  (Q9U1G7_FASHE) -  Thioredoxin from Fasciola hepatica

Seq: 104 a.a.

Struc: 104 a.a.

Enzyme reactions

• Enzyme class: E.C.1.8.4.8 - phosphoadenylyl-sulfate reductase (thioredoxin).
• Reaction: [thioredoxin]-disulfide + sulfite + adenosine 3',5'-bisphosphate + 2 H⁺ = [thioredoxin]-dithiol + 3'-phosphoadenylyl sulfate

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

reference

DOI no: 10.1016/j.molbiopara.2008.06.009

Mol Biochem Parasitol 161:44-48 (2008)

PubMed id: 18620002

The Fasciola hepatica thioredoxin: High resolution structure reveals two oxidation states.

K.Line, M.N.Isupov, E.Garcia-Rodriguez, G.Maggioli, F.Parra, J.A.Littlechild.

ABSTRACT

The Fasciola hepatica thioredoxin protein structure has been determined to 1.45A resolution. This is the first example of a single crystal structure to show the active site cysteine residues in both the reduced and disulfide oxidised form. Consistent with this observation the process of oxidation appears to require very little rearrangement of the surrounding protein structure. The F. hepatica thioredoxin structure has been compared to other thioredoxin protein structures already known and is found to be highly conserved. The F. hepatica protein is most similar to that of the thioredoxin from its human and animal hosts but it resembles other parasitic thioredoxins with regard to having no additional cysteine residues and is therefore not regulated by transient disulfide bond formation as proposed for thioredoxins from higher eukaryotic species.