Open AccessCrystallization and preliminary X‐ray analysis of 6‐hydroxymethyl‐7,8‐dihydropterin pyrophosphokinase from Staphylococcus aureus
Author(s) -
Chhabra Sandeep,
Newman Janet,
Peat Thomas S.,
Fernley Ross T.,
Caine Joanne,
Simpson Jamie S.,
Swarbrick James D.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110010857
Subject(s) - hydroxymethyl , crystallization , malonate , crystallography , pyrophosphate , ammonium sulfate , chemistry , solvent , molecule , stereochemistry , biochemistry , organic chemistry , enzyme
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 Å resolution. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 36.8, b = 76.6, c = 51.5 Å, α = γ = 90.0, β = 100.2°. The crystals contained two molecules per asymmetric unit, with a volume per protein weight ( V M ) of 2.04 Å 3 Da −1 and an estimated solvent content of 39.6%.