Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori.
Phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3) is an essential enzyme in the coenzyme A (CoA) biosynthetic pathway and catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA. PPAT from Helicobacter pylori has been overexpressed in Escherichia coli and crystallized at 296 K using sodium chloride as a precipitant by the hanging-drop vapour-diffusion method. X-ray diffraction data have been collected to 2.00 A resolution at 100 K using synchrotron radiation. The crystals belong to the trigonal space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 80.50, c = 143.05 A, alpha = beta = 90, gamma = 120 degrees. Six monomers of PPAT are likely to be present in the asymmetric unit, giving a V(M) of 2.39 A(3) Da(-1) and a solvent content of 49%.
Eom
Su Jeong
SJ
Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
Ahn
Hyung Jun
HJ
Kim
Hyung Wook
HW
Baek
Seung-Hun
SH
Suh
Se Won
SW
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology*; D009713:Nucleotidyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D009713:Nucleotidyltransferases; C022315:pantetheine-phosphate adenylyltransferase