1ZZ7

Crystal Structure of FeII HppE in Complex with Substrate form 1

Summary for 1ZZ7

• Entry DOI: 10.2210/pdb1zz7/pdb
• Related: 1ZZ6 1ZZ8 1ZZ9 1ZZB 1ZZC
• Descriptor: Hydroxyprophylphosphonic Acid Epoxidase, FE (II) ION, (S)-2-HYDROXYPROPYLPHOSPHONIC ACID, ... (4 entities in total)
• Functional Keywords: substrate-enzyme complex, cupin, mononuclear iron enzyme, oxidoreductase
• Biological source: Streptomyces wedmorensis
• Total number of polymer chains: 2
• Total formula weight: 43114.09

Authors

Higgins, L.J.,Yan, F.,Liu, P.,Liu, H.W.,Drennan, C.L. (deposition date: 2005-06-13, release date: 2005-07-26, Last modification date: 2023-08-23)

Primary citation

Higgins, L.J.,Yan, F.,Liu, P.,Liu, H.W.,Drennan, C.L.
Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme
Nature, 437:838-844, 2005

PubMed Abstract: 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.

PubMed: 16015285
DOI: 10.1038/nature03924

Experimental method

X-RAY DIFFRACTION (2.1 Å)