PDBsum entry: 1okg

Transferase

PDB id: 1okg

Contents

Protein chain

362 a.a. *

Ligands

SO3

Metals

_CA

Waters ×404

* Residue conservation analysis

PDB id:

1okg

Name:

Transferase

Title:

3-mercaptopyruvate sulfurtransferase from leishmania major

Structure:

Possible 3-mercaptopyruvate sulfurtransferase. Chain: a. Synonym: mercaptopyruvate sulfurtransferase. Engineered: yes. Mutation: yes

Source:

Leishmania major. Organism_taxid: 5664. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Monomer (from PDB file)

Resolution:

2.10Å R-factor: 0.212 R-free: 0.287

Authors:

M.S.Alphey,W.N.Hunter

Key ref:

M.S.Alphey et al. (2003). The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active site. J Biol Chem, 278, 48219-48227. PubMed id: 12952945 DOI: 10.1074/jbc.M307187200

Date:

24-Jul-03 Release date: 11-Sep-03

Protein chain

Q9NE49  (Q9NE49_LEIMA) -

 Gene Ontology (GO) functional annotation 

• Biochemical function: transferase activity (2 terms)

DOI no: 10.1074/jbc.M307187200

J Biol Chem 278:48219-48227 (2003)

PubMed id: 12952945

The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active site.

M.S.Alphey, R.A.Williams, J.C.Mottram, G.H.Coombs, W.N.Hunter.

ABSTRACT

Leishmania major 3-mercaptopyruvate sulfurtransferase is a crescent-shaped molecule comprising three domains. The N-terminal and central domains are similar to the thiosulfate sulfurtransferase rhodanese and create the active site containing a persulfurated catalytic cysteine (Cys-253) and an inhibitory sulfite coordinated by Arg-74 and Arg-185. A serine protease-like triad, comprising Asp-61, His-75, and Ser-255, is near Cys-253 and represents a conserved feature that distinguishes 3-mercaptopyruvate sulfurtransferases from thiosulfate sulfurtransferases. During catalysis, Ser-255 may polarize the carbonyl group of 3-mercaptopyruvate to assist thiophilic attack, whereas Arg-74 and Arg-185 bind the carboxylate group. The enzyme hydrolyzes benzoyl-Arg-p-nitroanilide, an activity that is sensitive to the presence of the serine protease inhibitor N alpha-p-tosyl-L-lysine chloromethyl ketone, which also lowers 3-mercaptopyruvate sulfurtransferase activity, presumably by interference with the contribution of Ser-255. The L. major 3-mercaptopyruvate sulfurtransferase is unusual with an 80-amino acid C-terminal domain, bearing remarkable structural similarity to the FK506-binding protein class of peptidylprolyl cis/trans-isomerase. This domain may be involved in mediating protein folding and sulfurtransferase-protein interactions.

Selected figure(s)

Figure 3.
FIG. 3. a, stereo view depicting superposition of C- traces of LmMST (red) and bovine rhodanese (Protein Data Bank code 1RHS [PDB] ). The N-terminal domain of LmMST is cyan; the central domain is blue; and the C-terminal domain is red. The trace for rhodanese is magenta. The view is the same as in Fig. 2a. b, stereo view of the two rhodanese-like domains of LmMST superimposed. The N-terminal domain is colored cyan, and the central domain is blue. The active-site Cys-253 and the spatially equivalent N-terminal Asp-102 are included.

Figure 4.
FIG. 4. Stereo view of the LmMST C-terminal domain superimposed onto the catalytic domain of FKBP (Protein Data Bank code 1FKJ [PDB] ). LmMST is shown in red, and FKBP in blue. C- atoms of LmMST are numbered. The positions of Cys-331 in LmMST and the inhibitor FK506 (black sticks) bound to FKBP are also shown.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2003, 278, 48219-48227) copyright 2003.

Figures were selected by the author.