Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 01; 67(Pt 1):38-40.AC
Abstract
Quinolinate phosphoribosyltransferase (QPRTase) is a key NAD-biosynthetic enzyme which catalyzes the transfer of quinolinic acid to 5-phosphoribosyl-1-pyrophosphate, yielding nicotinic acid mononucleotide. Homo sapiens QPRTase (Hs-QPRTase) appeared as a hexamer during purification and the protein was crystallized. Diffraction data were collected and processed at 2.8 Å resolution. Native Hs-QPRTase crystals belonged to space group P2(1), with unit-cell parameters a=76.2, b=137.1, c=92.7 Å, β=103.8°. Assuming the presence of six molecules in the asymmetric unit, the calculated Matthews coefficient is 2.46 Å3 Da(-1), which corresponds to a solvent content of 49.9%.
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MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
21206019
Citation
Kang, Gil Bu, et al. "Crystallization and Preliminary X-ray Crystallographic Analysis of Human Quinolinate Phosphoribosyltransferase." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 67, no. Pt 1, 2011, pp. 38-40.
Kang GB, Kim MK, Youn HS, et al. Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011;67(Pt 1):38-40.
Kang, G. B., Kim, M. K., Youn, H. S., An, J. Y., Lee, J. G., Park, K. R., Lee, S. H., Kim, Y., Fukuoka, S., & Eom, S. H. (2011). Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 67(Pt 1), 38-40. https://doi.org/10.1107/S1744309110041011
Kang GB, et al. Crystallization and Preliminary X-ray Crystallographic Analysis of Human Quinolinate Phosphoribosyltransferase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):38-40. PubMed PMID: 21206019.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.
AU - Kang,Gil Bu,
AU - Kim,Mun-Kyoung,
AU - Youn,Hyung-Seop,
AU - An,Jun Yop,
AU - Lee,Jung-Gyu,
AU - Park,Kyoung Ryoung,
AU - Lee,Sung Hang,
AU - Kim,Yongseong,
AU - Fukuoka,Shin-Ichi,
AU - Eom,Soo Hyun,
Y1 - 2010/12/21/
PY - 2010/01/20/received
PY - 2010/10/12/accepted
PY - 2011/1/6/entrez
PY - 2011/1/6/pubmed
PY - 2011/4/13/medline
SP - 38
EP - 40
JF - Acta crystallographica. Section F, Structural biology and crystallization communications
JO - Acta Crystallogr Sect F Struct Biol Cryst Commun
VL - 67
IS - Pt 1
N2 - Quinolinate phosphoribosyltransferase (QPRTase) is a key NAD-biosynthetic enzyme which catalyzes the transfer of quinolinic acid to 5-phosphoribosyl-1-pyrophosphate, yielding nicotinic acid mononucleotide. Homo sapiens QPRTase (Hs-QPRTase) appeared as a hexamer during purification and the protein was crystallized. Diffraction data were collected and processed at 2.8 Å resolution. Native Hs-QPRTase crystals belonged to space group P2(1), with unit-cell parameters a=76.2, b=137.1, c=92.7 Å, β=103.8°. Assuming the presence of six molecules in the asymmetric unit, the calculated Matthews coefficient is 2.46 Å3 Da(-1), which corresponds to a solvent content of 49.9%.
SN - 1744-3091
UR - https://www.unboundmedicine.com/medline/citation/21206019/Crystallization_and_preliminary_X_ray_crystallographic_analysis_of_human_quinolinate_phosphoribosyltransferase_
L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309110041011
DB - PRIME
DP - Unbound Medicine
ER -