1iho

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spinqualitylabelsall models 1iho, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI

Overview

BACKGROUND: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the, pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the, condensation of pantoate with beta-alanine in an ATP-dependent reaction., RESULTS: We describe the overexpression, purification, and crystal, structure of recombinant pantothenate synthetase from E. coli. The, structure was solved by a selenomethionine multiwavelength anomalous, dispersion experiment and refined against native data to a final R(cryst), of 22.6% (R(free) = 24.9%) at 1.7 A resolution. The enzyme is dimeric, with two well-defined domains per protomer: the N-terminal domain, a, Rossmann fold, contains the active site cavity, with the C-terminal domain, forming a hinged lid. CONCLUSIONS: The N-terminal domain is structurally, very similar to class I aminoacyl-tRNA synthetases and is thus a member of, the cytidylyltransferase superfamily. This relationship has been used to, suggest the location of the ATP and pantoate binding sites and the nature, of hinge bending that leads to the ternary enzyme-pantoate-ATP complex.

About this Structure

1IHO is a Single protein structure of sequence from Escherichia coli with TRS and EDO as ligands. Active as Pantoate--beta-alanine ligase, with EC number 6.3.2.1 Full crystallographic information is available from OCA.

Reference

The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily., von Delft F, Lewendon A, Dhanaraj V, Blundell TL, Abell C, Smith AG, Structure. 2001 May 9;9(5):439-50. PMID:11377204

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