Rhombohedral crystals of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase.
The penultimate step of prokaryotic coenzyme A (CoA) biosynthesis is directed by the essential enzyme phosphopantetheine adenylyltransferase (PPAT; EC 2.7.7.3), an attractive target for antibiotics. The reaction catalyzed by PPAT is rate-limiting and involves the transfer of an adenylyl group from ATP to 4'-phosphopantetheine to form 3'-dephospho-CoA. Rhombohedral crystals of PPAT from Mycobacterium tuberculosis (Rv2965c) were obtained. The crystals belong to space group R32, with unit-cell parameters a = 68.69 A, alpha = 91.81 degrees. The crystals diffract to better than 2 A resolution on a Cu Kalpha rotating-anode generator. The packing density for one polypeptide chain in the asymmetric unit is 2.89 A(3) Da(-1), with a solvent content of 0.57.
Brown
Kathrin L
KL
Department of Hematology-Oncology, St Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Morris
Van K
VK
Izard
Tina
T
D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009713:Nucleotidyltransferases / Q000737:chemistry*
D001426:Bacterial Proteins; D009713:Nucleotidyltransferases; C022315:pantetheine-phosphate adenylyltransferase