2jg2
From Proteopedia
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HIGH RESOLUTION STRUCTURE OF SPT WITH PLP INTERNAL ALDIMINE
Overview
Sphingolipid biosynthesis commences with the condensation of L-serine and, palmitoyl-CoA to produce 3-ketodihydrosphingosine (KDS). This reaction is, catalysed by the PLP-dependent enzyme serine palmitoyltransferase (SPT; EC, 2.3.1.50), which is a membrane-bound heterodimer (SPT1/SPT2) in eukaryotes, such as humans and yeast and a cytoplasmic homodimer in the Gram-negative, bacterium Sphingomonas paucimobilis. Unusually, the outer membrane of S., paucimobilis contains glycosphingolipid (GSL) instead of, lipopolysaccharide (LPS), and SPT catalyses the first step of the GSL, biosynthetic pathway in this organism. We report here the crystal, structure of the holo-form of S. paucimobilis SPT at 1.3 A resolution. The, enzyme is a symmetrical homodimer with two active sites and a monomeric, ... [(full description)]
About this Structure
2JG2 is a [Single protein] structure of sequence from [Pseudomonas paucimobilis] with MG as [ligand]. Active as [[1]], with EC number [2.3.1.50]. Full crystallographic information is available from [OCA].
Reference
The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis., Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ, J Mol Biol. 2007 Jul 27;370(5):870-86. Epub 2007 May 10. PMID:17559874
Page seeded by OCA on Mon Oct 29 20:54:40 2007
Categories: Pseudomonas paucimobilis | Single protein | Barton, G.J. | Campopiano, D.J. | Carter, L.G. | Dorward, M. | Johnson, K.A. | Liu, H. | Mcmahon, S.A. | Naismith, J.H. | Oke, M. | Overton, I.M. | Puech, D. | Yard, B.A. | MG | Plp | Pyridoxal phosphate | Serine palmitoyl transferase | Sphingolipid | Spt | Sspf | Transferase
