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Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori.
Acta Crystallogr D Biol Crystallogr. 2003 Mar; 59(Pt 3):561-2.AC

Abstract

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%.

Authors+Show Affiliations

Structural Proteomics Laboratory, School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12595726

Citation

Eom, Su Jeong, et al. "Crystallization and Preliminary X-ray Crystallographic Studies of Phosphopantetheine Adenylyltransferase From Helicobacter Pylori." Acta Crystallographica. Section D, Biological Crystallography, vol. 59, no. Pt 3, 2003, pp. 561-2.
Eom SJ, Ahn HJ, Kim HW, et al. Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori. Acta Crystallogr D Biol Crystallogr. 2003;59(Pt 3):561-2.
Eom, S. J., Ahn, H. J., Kim, H. W., Baek, S. H., & Suh, S. W. (2003). Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori. Acta Crystallographica. Section D, Biological Crystallography, 59(Pt 3), 561-2.
Eom SJ, et al. Crystallization and Preliminary X-ray Crystallographic Studies of Phosphopantetheine Adenylyltransferase From Helicobacter Pylori. Acta Crystallogr D Biol Crystallogr. 2003;59(Pt 3):561-2. PubMed PMID: 12595726.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori. AU - Eom,Su Jeong, AU - Ahn,Hyung Jun, AU - Kim,Hyung Wook, AU - Baek,Seung-Hun, AU - Suh,Se Won, Y1 - 2003/02/21/ PY - 2002/10/09/received PY - 2003/01/02/accepted PY - 2003/2/22/pubmed PY - 2003/10/8/medline PY - 2003/2/22/entrez SP - 561 EP - 2 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 59 IS - Pt 3 N2 - 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%. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/12595726/Crystallization_and_preliminary_X_ray_crystallographic_studies_of_phosphopantetheine_adenylyltransferase_from_Helicobacter_pylori_ DB - PRIME DP - Unbound Medicine ER -