1m3u

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spinqualitylabelsall models 1m3u, resolution 1.800Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate

Overview

We report the crystal structure of E. coli ketopantoate, hydroxymethyltransferase (KPHMT) at 1.9 A resolution, in complex with its, product, ketopantoate. KPHMT catalyzes the first step in the biosynthesis, of pantothenate (vitamin B(5)), the precursor of coenzyme A and the acyl, carrier protein cofactor. The structure of the decameric enzyme was solved, by multiwavelength anomalous dispersion to locate 160 selenomethionine, sites and phase 560 kDa of protein, making it the largest structure solved, by this approach. KPHMT adopts the (betaalpha)(8) barrel fold and is a, member of the phosphoenolpyruvate/pyruvate superfamily. The active site, contains a ketopantoate bidentately coordinated to Mg(2+). Similar binding, is likely for the substrate, alpha-ketoisovalerate, orienting the C3 for, deprotonation.

About this Structure

1M3U is a Single protein structure of sequence from Escherichia coli with MG and KPL as ligands. Active as 3-methyl-2-oxobutanoate hydroxymethyltransferase, with EC number 2.1.2.11 Full crystallographic information is available from OCA.

Reference

Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites., von Delft F, Inoue T, Saldanha SA, Ottenhof HH, Schmitzberger F, Birch LM, Dhanaraj V, Witty M, Smith AG, Blundell TL, Abell C, Structure. 2003 Aug;11(8):985-96. PMID:12906829

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