1OKG

3-mercaptopyruvate sulfurtransferase from Leishmania major

Summary for 1OKG

• Entry DOI: 10.2210/pdb1okg/pdb
• Descriptor: POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE, CALCIUM ION, SULFITE ION, ... (4 entities in total)
• Functional Keywords: mercaptopyruvate, sulfurtransferase, rhodanese, prolyl isomerase, catalytic triad, serine protease, leishmania pyruvate, transferase
• Biological source: LEISHMANIA MAJOR
• Total number of polymer chains: 1
• Total formula weight: 41417.83

Authors

Alphey, M.S.,Hunter, W.N. (deposition date: 2003-07-24, release date: 2003-09-11, Last modification date: 2024-10-16)

Primary citation

Alphey, M.S.,Williams, R.A.M.,Mottram, J.C.,Coombs, G.H.,Hunter, W.N.
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-, 2003

PubMed 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.

PubMed: 12952945
DOI: 10.1074/JBC.M307187200

Experimental method

X-RAY DIFFRACTION (2.1 Å)