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Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide.
- Source :
-
Acta Crystallographica: Section F (Wiley-Blackwell) . Dec2012, Vol. 68 Issue 12, p1488-1490. 3p. 2 Color Photographs, 2 Diagrams, 1 Chart. - Publication Year :
- 2012
-
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 ų Da-1 and 60.3%, respectively, assuming the presence of two molecules in the asymmetric unit. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 68
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 161107004
- Full Text :
- https://doi.org/10.1107/S1744309112040638