PDBsum entry: 1rxe

Oxidoreductase

PDB id: 1rxe

Contents

Protein chain

131 a.a. *

Ligands

LCP

MNB

Metals

__K

Waters ×125

* Residue conservation analysis

PDB id:

1rxe

Name:

Oxidoreductase

Title:

Arsc complexed with mnb

Structure:

Arsenate reductase. Chain: a. Synonym: arsc, arsenical pump modifier. Engineered: yes. Mutation: yes

Source:

Staphylococcus aureus. Organism_taxid: 1280. Gene: arsc, sap018. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.70Å R-factor: 0.195 R-free: 0.212

Authors:

J.Messens,I.Van Molle,P.Vanhaesebrouck,M.Limbourg,K.Van Belle,K.Wahni,J.C.Martins,R.Loris,L.Wyns

Key ref:

J.Messens et al. (2004). The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct. Acta Crystallogr D Biol Crystallogr, 60, 1180-1184. PubMed id: 15159594 DOI: 10.1107/S0907444904007334

Date:

18-Dec-03 Release date: 01-Jun-04

Protein chain

P0A006  (ARSC_STAAU) -  Protein ArsC

Seq: 131 a.a.

Struc: 131 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate

Protein tyrosine phosphate + H(2)O = protein tyrosine (Bound ligand (Het Group name = MNB) matches with 42.00% similarity) + phosphate

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

 Gene Ontology (GO) functional annotation 

• Biological process: oxidation reduction (3 terms)
• Biochemical function: oxidoreductase activity (4 terms)

reference

DOI no: 10.1107/S0907444904007334

Acta Crystallogr D Biol Crystallogr 60:1180-1184 (2004)

PubMed id: 15159594

The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.

J.Messens, I.Van Molle, P.Vanhaesebrouck, K.Van Belle, K.Wahni, J.C.Martins, L.Wyns, R.Loris.

ABSTRACT

Structural insights into formation of the complex between the ubiquitous thiol-disulfide oxidoreductase thioredoxin and its oxidized substrate are under-documented owing to its entropical instability. In vitro, it is possible via a reaction with 5,5'-dithiobis-(2-nitrobenzoic acid) to make a stable mixed-disulfide complex between thioredoxin from Staphylococcus aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC) from S. aureus. In the absence of the crystal structure of an ArsC-thioredoxin complex, the structures of two precursors of the complex, the ArsC triple mutant ArsC C10SC15AC82S and its 5-thio-2-nitrobenzoic acid (TNB) adduct, were determined. The ArsC triple mutant has a structure very similar to that of the reduced form of wild-type ArsC, with a folded redox helix and a buried catalytic Cys89. In the adduct form, the TNB molecule is buried in a hydrophobic pocket and the disulfide bridge between TNB and Cys89 is sterically inaccessible to thioredoxin. In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary.

Selected figure(s)

Figure 1.
Figure 1 (a) The structure of wild-type ArsC in the reduced state (PDB code [38]1ljl ). The short redox helix bearing Cys82 and Cys89 (green) is structured. (b) The structure of ArsC C15A in the oxidized state (PDB code [39]1lju ). The short redox helix is looped-out (green). In this structure, arsenite is bound in the active site P-loop. In both structures, the redox-active cysteines (in stick representation) and the P-loop active site (red) are shown. The figures were prepared using the program PyMol 0.9 (DeLano Scientific).

Figure 4.
Figure 4 (a) F[o] - F[c] omit electron-density map of 5-thio-2-nitrobenzoate (TNB) bound to Cys89 in the structure of C10SC15AC82S (PDB code [117]1rxe ) at 1.7 Å. The map is contoured at 3.0 [118][sigma] . Figure prepared using the program MOLSCRIPT (Kraulis, 1991[119] [Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]-[120][bluearr.gif] ). (b) The TNB molecule as observed in its structural hydrophobic environment. The figure was prepared using PyMol 0.9 (DeLano Scientific).

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1180-1184) copyright 2004.

Figures were selected by an automated process.