Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide.

Hyung-Seop Youn, Mun-Kyoung Kim, Gil Bu Kang, Tae Gyun Kim, Jun Yop An, Jung-Gyu Lee, Kyoung Ryoung Park, Youngjin Lee, Shin-Ichi Fukuoka, Soo Hyun Eom

Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68(Pt 12) , 1488-90, (2012)

Full Text: HTML

Abstract

Quinolinate phosphoribosyltransferase (QAPRTase) is a key enzyme in NAD biosynthesis; it catalyzes the formation of nicotinate mononucleotide (NAMN) from quinolinate and 5-phosphoribosyl-1-pyrophosphate. In order to elucidate the mechanism of NAMN biosynthesis, crystals of Sus scrofa QAPRTase (Ss-QAPRTase) purified from porcine kidney in complex with NAMN were obtained and diffraction data were collected and processed to 2.1 Å resolution. The Ss-QAPRTase-NAMN cocrystals belonged to space group P321, with unit-cell parameters a=119.1, b=119.1, c=93.7 Å, γ=120.0°. The Matthews coefficient and the solvent content were estimated as 3.10 Å3 Da(-1) and 60.3%, respectively, assuming the presence of two molecules in the asymmetric unit.