1zzc: Difference between revisions

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==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.

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==

Line 13:

[[Category: Single protein]]

[[Category: Streptomyces wedmorensis]]

[[Category: Drennan, C.L.]]

[[Category: Drennan, C L.]]

[[Category: Higgins, L.J.]]

[[Category: Higgins, L J.]]

[[Category: Liu, H.W.]]

[[Category: Liu, H W.]]

[[Category: Liu, P.]]

[[Category: Yan, F.]]

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[[Category: mononuclear iron enzyme]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Streptomyces wedmorensis]]
-[[Category: Drennan, C.L.]]
+[[Category: Drennan, C L.]]
-[[Category: Higgins, L.J.]]
+[[Category: Higgins, L J.]]
-[[Category: Liu, H.W.]]
+[[Category: Liu, H W.]]
 [[Category: Liu, P.]]
 [[Category: Yan, F.]]
@@ Line 24: / Line 24: @@
 [[Category: mononuclear iron enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:46:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:34 2008''