4FYM

Crystal structure of Plasmodium falciparum orotate phosphoribosyltransferase

Summary for 4FYM

• Entry DOI: 10.2210/pdb4fym/pdb
• Descriptor: Orotate phosphoribosyltransferase, SULFATE ION (3 entities in total)
• Functional Keywords: rossmann fold, transferase
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 8
• Total formula weight: 254582.95

Authors

Rathod, P.K.,Kumar, S. (deposition date: 2012-07-05, release date: 2013-08-07, Last modification date: 2024-02-28)

Primary citation

Kumar, S.,Krishnamoorthy, K.,Mudeppa, D.G.,Rathod, P.K.
Structure of Plasmodium falciparum orotate phosphoribosyltransferase with autologous inhibitory protein-protein interactions.
Acta Crystallogr F Struct Biol Commun, 71:600-608, 2015

PubMed Abstract: The most severe form of malaria is caused by the obligate parasite Plasmodium falciparum. Orotate phosphoribosyltransferase (OPRTase) is the fifth enzyme in the de novo pyrimidine-synthesis pathway in the parasite, which lacks salvage pathways. Among all of the malaria de novo pyrimidine-biosynthesis enzymes, the structure of P. falciparum OPRTase (PfOPRTase) was the only one unavailable until now. PfOPRTase that could be crystallized was obtained after some low-complexity sequences were removed. Four catalytic dimers were seen in the asymmetic unit (a total of eight polypeptides). In addition to revealing unique amino acids in the PfOPRTase active sites, asymmetric dimers in the larger structure pointed to novel parasite-specific protein-protein interactions that occlude the catalytic active sites. The latter could potentially modulate PfOPRTase activity in parasites and possibly provide new insights for blocking PfOPRTase functions.

PubMed: 25945715
DOI: 10.1107/S2053230X1500549X

Experimental method

X-RAY DIFFRACTION (2.6 Å)