1zzc

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Revision as of 15:46, 29 January 2008

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spinqualitylabelsall models 1zzc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of CoII HppE in Complex with Tris Buffer

Overview

The biosynthetic pathway of the clinically important antibiotic fosfomycin, uses enzymes that catalyse reactions without precedent in biology. Among, these is hydroxypropylphosphonic acid epoxidase, which represents a new, subfamily of non-haem mononuclear iron enzymes. Here we present six X-ray, structures of this enzyme: the apoenzyme at 2.0 A resolution; a native, Fe(II)-bound form at 2.4 A resolution; a, tris(hydroxymethyl)aminomethane-Co(II)-enzyme complex structure at 1.8 A, resolution; a substrate-Co(II)-enzyme complex structure at 2.5 A, resolution; and two substrate-Fe(II)-enzyme complexes at 2.1 and 2.3 A, resolution. These structural data lead us to suggest how this enzyme is, able to recognize and respond to its substrate with a conformational, change that protects the radical-based intermediates formed during, catalysis. Comparisons with other family members suggest why substrate, binding is able to prime iron for dioxygen binding in the absence of, alpha-ketoglutarate (a co-substrate required by many mononuclear iron, enzymes), and how the unique epoxidation reaction of, hydroxypropylphosphonic acid epoxidase may occur.

About this Structure

1ZZC is a Single protein structure of sequence from Streptomyces wedmorensis with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme., Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL, Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285

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