1od6: Difference between revisions

Revision as of 15:16, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1OD6 is a Single protein structure of sequence from Thermus thermophilus with and as ligands. Active as Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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 ==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 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.
+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.
 ==About this Structure==
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 [[Category: Inagaki, E.]]
 [[Category: Miyano, M.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Tahirov, T.]]
 [[Category: Takahashi, H.]]
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 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:56:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:17 2008''