2jg2

From Proteopedia

Revision as of 15:28, 30 October 2007

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 [Sphingomonas paucimobilis] with MG as [ligand]. Active as [Serine C-palmitoyltransferase], with EC number [2.3.1.50]. Structure known Active Site: AC1. 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

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