Crystal structure of Leishmania tarentolae hypoxanthine-guanine phosphoribosyltransferase.

ABSTRACT:

Background

Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (EC 2.4.2.8) is a central enzyme in the purine recycling pathway. Parasitic protozoa of the order Kinetoplastida cannot synthesize purines de novo and use the salvage pathway to synthesize purine bases, making this an attractive target for antiparasitic drug design.

Results

The glycosomal HGPRT from Leishmania tarentolae in a catalytically active form purified and co-crystallized with a guanosine monophosphate (GMP) in the active site. The dimeric structure of HGPRT has been solved by molecular replacement and refined against data extending to 2.1 A resolution. The structure reveals the contacts of the active site residues with GMP.

Conclusion

Comparative analysis of the active sites of Leishmania and h

SUBMITTER: Monzani PS 

PROVIDER: S-EPMC2228302 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature