1zz7
From Proteopedia
(New page: 200px<br /><applet load="1zz7" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zz7, resolution 2.10Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | The biosynthetic pathway of the clinically important antibiotic fosfomycin | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces wedmorensis]] | [[Category: Streptomyces wedmorensis]] | ||
| - | [[Category: Drennan, C | + | [[Category: Drennan, C L.]] |
| - | [[Category: Higgins, L | + | [[Category: Higgins, L J.]] |
| - | [[Category: Liu, H | + | [[Category: Liu, H W.]] |
[[Category: Liu, P.]] | [[Category: Liu, P.]] | ||
[[Category: Yan, F.]] | [[Category: Yan, F.]] | ||
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[[Category: substrate-enzyme complex]] | [[Category: substrate-enzyme complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:30 2008'' |
Revision as of 14:20, 21 February 2008
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Crystal Structure of FeII HppE in Complex with Substrate form 1
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
1ZZ7 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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