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Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.

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, ?=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%.

SUBMITTER: Kang GB

PROVIDER: S-EPMC3079967 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.

Kang Gil Bu GB Kim Mun-Kyoung MK Youn Hyung-Seop HS An Jun Yop JY Lee Jung-Gyu JG Park Kyoung Ryoung KR Lee Sung Hang SH Kim Yongseong Y Fukuoka Shin-Ichi S Eom Soo Hyun SH

Acta crystallographica. Section F, Structural biology and crystallization communications 20101221 Pt 1

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. ...[more]

PMID: 21206019

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