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Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 01; 68(Pt 12):1488-90.AC

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.

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Authors+Show Affiliations

Youn HS
School of Life Sciences, Cell Dynamics Research Center, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
Kim MK
No affiliation info available
Kang GB
No affiliation info available
Kim TG
No affiliation info available
An JY
No affiliation info available
Lee JG
No affiliation info available
Park KR
No affiliation info available
Lee Y
No affiliation info available
Fukuoka S
No affiliation info available
Eom SH
No affiliation info available

MeSH

AnimalsCrystallography, X-RayKidneyModels, MolecularNicotinamide MononucleotidePentosyltransferasesProtein ConformationSwine

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23192029

Citation

Youn, Hyung-Seop, et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of Quinolinate Phosphoribosyltransferase From Porcine Kidney in Complex With Nicotinate Mononucleotide." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 68, no. Pt 12, 2012, pp. 1488-90.
Youn HS, Kim MK, Kang GB, et al. Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68(Pt 12):1488-90.
Youn, H. S., Kim, M. K., Kang, G. B., Kim, T. G., An, J. Y., Lee, J. G., Park, K. R., Lee, Y., Fukuoka, S., & Eom, S. H. (2012). Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 68(Pt 12), 1488-90. https://doi.org/10.1107/S1744309112040638
Youn HS, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of Quinolinate Phosphoribosyltransferase From Porcine Kidney in Complex With Nicotinate Mononucleotide. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1488-90. PubMed PMID: 23192029.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase from porcine kidney in complex with nicotinate mononucleotide. AU - Youn,Hyung-Seop, AU - Kim,Mun-Kyoung, AU - Kang,Gil Bu, AU - Kim,Tae Gyun, AU - An,Jun Yop, AU - Lee,Jung-Gyu, AU - Park,Kyoung Ryoung, AU - Lee,Youngjin, AU - Fukuoka,Shin-Ichi, AU - Eom,Soo Hyun, Y1 - 2012/11/14/ PY - 2012/09/19/received PY - 2012/09/26/accepted PY - 2012/11/30/entrez PY - 2012/11/30/pubmed PY - 2013/5/15/medline SP - 1488 EP - 90 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 68 IS - Pt 12 N2 - 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. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/23192029/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_quinolinate_phosphoribosyltransferase_from_porcine_kidney_in_complex_with_nicotinate_mononucleotide_ L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309112040638 DB - PRIME DP - Unbound Medicine ER -