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| [[Image:1zzc.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1zzc| PDB=1zzc | SCENE= }} | | {{STRUCTURE_1zzc| PDB=1zzc | SCENE= }} |
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| '''Crystal Structure of CoII HppE in Complex with Tris Buffer'''
| | ===Crystal Structure of CoII HppE in Complex with Tris Buffer=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_16015285}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16015285 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16015285}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Holo-hppe]] | | [[Category: Holo-hppe]] |
| [[Category: Mononuclear iron enzyme]] | | [[Category: Mononuclear iron enzyme]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:16:04 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:38:33 2008'' |
