Unknown

Dataset Information

0

Crystallization of human nicotinamide phosphoribosyltransferase.


ABSTRACT: In the NAD biosynthetic pathway, nicotinamide phosphoribosyltransferase (NMPRTase; EC 2.4.2.12) plays an important role in catalyzing the synthesis of nicotinamide mononucleotide from nicotinamide and 5'-phosphoribosyl-1'-pyrophosphate. Because the diffraction pattern of the initially obtained crystals was not suitable for structure analysis, the crystal quality was improved by successive use of the microseeding technique. The resultant crystals diffracted to 2.0 A resolution. These crystals belonged to space group P21, with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 A. Here, the crystallization of human NMPRTase is reported in the free form; the crystals should be useful for inhibitor-soaking experiments on the enzyme.

SUBMITTER: Takahashi R 

PROVIDER: S-EPMC2335003 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystallization of human nicotinamide phosphoribosyltransferase.

Takahashi Ryo R   Nakamura Shota S   Yoshida Takuya T   Kobayashi Yuji Y   Ohkubo Tadayasu T  

Acta crystallographica. Section F, Structural biology and crystallization communications 20070406 Pt 5


In the NAD biosynthetic pathway, nicotinamide phosphoribosyltransferase (NMPRTase; EC 2.4.2.12) plays an important role in catalyzing the synthesis of nicotinamide mononucleotide from nicotinamide and 5'-phosphoribosyl-1'-pyrophosphate. Because the diffraction pattern of the initially obtained crystals was not suitable for structure analysis, the crystal quality was improved by successive use of the microseeding technique. The resultant crystals diffracted to 2.0 A resolution. These crystals bel  ...[more]

Similar Datasets

| S-EPMC3227030 | biostudies-literature
| S-EPMC3627370 | biostudies-literature
| S-EPMC7735423 | biostudies-literature
2021-11-20 | GSE189104 | GEO
| S-EPMC5614834 | biostudies-literature
| S-EPMC7464552 | biostudies-literature
| S-EPMC3469563 | biostudies-literature