1OD6

The Crystal Structure of Phosphopantetheine adenylyltransferase from Thermus Thermophilus in complex with 4'-phosphopantetheine

Summary for 1OD6

• Entry DOI: 10.2210/pdb1od6/pdb
• Related: 1B6T 1GN8 1H1T 1QJC
• Descriptor: PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE, 4'-PHOSPHOPANTETHEINE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: coenzyme a biosynthesis, transferase, nucleotidyltransferase, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: THERMUS THERMOPHILUS
• Cellular location: Cytoplasm : Q5SJS9
• Total number of polymer chains: 1
• Total formula weight: 18377.01

Authors

Takahashi, H.,Inagaki, E.,Miyano, M.,Tahirov, T.H. (deposition date: 2003-02-13, release date: 2003-03-13, Last modification date: 2023-12-13)

Primary citation

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, T.H.
Structure and Implications for the Thermal Stability of Phosphopantetheine Adenylyltransferase from Thermus Thermophilus.
Acta Crystallogr.,Sect.D, 60:97-, 2004

PubMed Abstract: 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 are conserved in Tt PPAT, indicating similarities in their substrate binding and enzymatic reaction. The notable difference between E. coli PPAT and Tt PPAT is the simultaneous substrate recognition by all six subunits of Tt PPAT compared with substrate recognition by only three subunits in E. coli PPAT. Comparative analysis also revealed that the higher stability of Tt PPAT arises from stabilization of each subunit by hydrophobic effects, hydrogen bonds and entropic effects.

PubMed: 14684898
DOI: 10.1107/S0907444903025319

Experimental method

X-RAY DIFFRACTION (1.5 Å)