2fct

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2fct" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fct, resolution 1.60&Aring;" /> '''SyrB2 with Fe(II), c...)
Line 4: Line 4:
==Overview==
==Overview==
-
Non-haem Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzymes harness, the reducing power of alphaKG to catalyse oxidative reactions, usually the, hydroxylation of unactivated carbons, and are involved in processes such, as natural product biosynthesis, the mammalian hypoxic response, and DNA, repair. These enzymes couple the decarboxylation of alphaKG with the, formation of a high-energy ferryl-oxo intermediate that acts as a, hydrogen-abstracting species. All previously structurally characterized, mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that, coordinates the iron. The two histidines and one carboxylate, known as the, 'facial triad', form one triangular side of an octahedral iron, coordination geometry. A subclass of mononuclear iron enzymes has been, shown to catalyse halogenation reactions, rather than the more typical, hydroxylation reaction. SyrB2, a member of this subclass, is a non-haem, Fe(II)/alphaKG-dependent halogenase that catalyses the chlorination of, threonine in syringomycin E biosynthesis. Here we report the structure of, SyrB2 with both a chloride ion and alphaKG coordinated to the iron ion at, 1.6 A resolution. This structure reveals a previously unknown coordination, of iron, in which the carboxylate ligand of the facial triad is replaced, by a chloride ion.
+
Non-haem Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzymes harness the reducing power of alphaKG to catalyse oxidative reactions, usually the hydroxylation of unactivated carbons, and are involved in processes such as natural product biosynthesis, the mammalian hypoxic response, and DNA repair. These enzymes couple the decarboxylation of alphaKG with the formation of a high-energy ferryl-oxo intermediate that acts as a hydrogen-abstracting species. All previously structurally characterized mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that coordinates the iron. The two histidines and one carboxylate, known as the 'facial triad', form one triangular side of an octahedral iron coordination geometry. A subclass of mononuclear iron enzymes has been shown to catalyse halogenation reactions, rather than the more typical hydroxylation reaction. SyrB2, a member of this subclass, is a non-haem Fe(II)/alphaKG-dependent halogenase that catalyses the chlorination of threonine in syringomycin E biosynthesis. Here we report the structure of SyrB2 with both a chloride ion and alphaKG coordinated to the iron ion at 1.6 A resolution. This structure reveals a previously unknown coordination of iron, in which the carboxylate ligand of the facial triad is replaced by a chloride ion.
==About this Structure==
==About this Structure==
Line 13: Line 13:
[[Category: Pseudomonas syringae pv. syringae]]
[[Category: Pseudomonas syringae pv. syringae]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Blasiak, L.C.]]
+
[[Category: Blasiak, L C.]]
-
[[Category: Drennan, C.L.]]
+
[[Category: Drennan, C L.]]
[[Category: AKG]]
[[Category: AKG]]
[[Category: CL]]
[[Category: CL]]
Line 23: Line 23:
[[Category: mononuclear iron]]
[[Category: mononuclear iron]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:33:24 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:03 2008''

Revision as of 15:20, 21 February 2008

Image:2fct.gif

2fct, resolution 1.60Å

Drag the structure with the mouse to rotate

SyrB2 with Fe(II), chloride, and alpha-ketoglutarate

Overview

Non-haem Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzymes harness the reducing power of alphaKG to catalyse oxidative reactions, usually the hydroxylation of unactivated carbons, and are involved in processes such as natural product biosynthesis, the mammalian hypoxic response, and DNA repair. These enzymes couple the decarboxylation of alphaKG with the formation of a high-energy ferryl-oxo intermediate that acts as a hydrogen-abstracting species. All previously structurally characterized mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that coordinates the iron. The two histidines and one carboxylate, known as the 'facial triad', form one triangular side of an octahedral iron coordination geometry. A subclass of mononuclear iron enzymes has been shown to catalyse halogenation reactions, rather than the more typical hydroxylation reaction. SyrB2, a member of this subclass, is a non-haem Fe(II)/alphaKG-dependent halogenase that catalyses the chlorination of threonine in syringomycin E biosynthesis. Here we report the structure of SyrB2 with both a chloride ion and alphaKG coordinated to the iron ion at 1.6 A resolution. This structure reveals a previously unknown coordination of iron, in which the carboxylate ligand of the facial triad is replaced by a chloride ion.

About this Structure

2FCT is a Single protein structure of sequence from Pseudomonas syringae pv. syringae with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis., Blasiak LC, Vaillancourt FH, Walsh CT, Drennan CL, Nature. 2006 Mar 16;440(7082):368-71. PMID:16541079

Page seeded by OCA on Thu Feb 21 17:20:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fct"
Personal tools