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. 2010 May 1;66(Pt 5):575-8.
doi: 10.1107/S1744309110010857. Epub 2010 Apr 30.

Crystallization and preliminary X-ray analysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Staphylococcus aureus

Sandeep Chhabra  1 , Janet Newman, Thomas S Peat, Ross T Fernley, Joanne Caine, Jamie S Simpson, James D Swarbrick
Affiliations

Crystallization and preliminary X-ray analysis of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Staphylococcus aureus

Sandeep Chhabra et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

Abstract

6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the Mg(2+)-dependent transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HMDP), forming 6-hydroxymethyl-7,8-dihydropterin pyrophosphate, which is a critical step in the de novo folic acid-biosynthesis pathway. Diffraction-quality crystals of HPPK from the medically relevant species Staphylococcus aureus were grown in the presence of ammonium sulfate or sodium malonate and diffracted to better than 1.65 A resolution. The crystals belonged to space group P2(1), with unit-cell parameters a = 36.8, b = 76.6, c = 51.5 A, alpha = gamma = 90.0, beta = 100.2 degrees . The crystals contained two molecules per asymmetric unit, with a volume per protein weight (V(M)) of 2.04 A(3) Da(-1) and an estimated solvent content of 39.6%.

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Figures

Figure 1
Figure 1
The folate pathway.
Figure 2
Figure 2
Diffraction image of a typical SaHPPK crystal.
Figure 3
Figure 3
Crystals of SaHPPK. The largest dimension of the central crystal shown is 0.143 mm.
See this image and copyright information in PMC

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