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spinqualitylabelsall models 1od6, resolution 1.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE CRYSTAL STRUCTURE OF PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE FROM THERMUS THERMOPHILUS IN COMPLEX WITH 4'-PHOSPHOPANTETHEINE

Overview

Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in, bacteria that catalyzes the rate-limiting step in coenzyme A (CoA), biosynthesis by transferring an adenylyl group from ATP to, 4'-phosphopantetheine (Ppant), yielding 3'-dephospho-CoA (dPCoA). The, crystal structure of PPAT from Thermus thermophilus HB8 (Tt PPAT), complexed with Ppant has been determined by the molecular-replacement, method at 1.5 A resolution. The overall fold of the enzyme is almost the, same as that of Escherichia coli PPAT, a hexamer having point group 32., The asymmetric unit of Tt PPAT contains a monomer and the crystallographic, triad and dyad coincide with the threefold and twofold axes of the, hexamer, respectively. Most of the important atoms surrounding the active, site in E. coli PPAT ... [(full description)]

About this Structure

1OD6 is a [Single protein] structure of sequence from [Thermus thermophilus] with SO4 and PNS as [ligands]. Active as [[1]], with EC number [2.7.7.3]. Full crystallographic information is available from [OCA].

Reference

Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus., Takahashi H, Inagaki E, Fujimoto Y, Kuroishi C, Nodake Y, Nakamura Y, Arisaka F, Yutani K, Kuramitsu S, Yokoyama S, Yamamoto M, Miyano M, Tahirov TH, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):97-104. Epub 2003, Dec 18. PMID:14684898

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