2f1d: Difference between revisions

Revision as of 18:16, 21 February 2008

X-Ray Structure of imidazoleglycerol-phosphate dehydratase

OverviewOverview

The structure of A. thaliana imidazoleglycerol-phosphate dehydratase, an enzyme of histidine biosynthesis and a target for the triazole phosphonate herbicides, has been determined to 3.0 A resolution. The structure is composed of 24 identical subunits arranged in 432 symmetry and shows how the formation of a novel dimanganese cluster is crucial to the assembly of the active 24-mer from an inactive trimeric precursor and to the formation of the active site of the enzyme. Molecular modeling suggests that the substrate is bound to the manganese cluster as an imidazolate moiety that subsequently collapses to yield a diazafulvene intermediate. The mode of imidazolate recognition exploits pseudosymmetry at the active site arising from a combination of the assembly of the particle and the pseudosymmetry present in each subunit as a result of gene duplication. This provides an intriguing example of the role of evolution in the design of Nature's catalysts.

About this StructureAbout this Structure

2F1D is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Active as Imidazoleglycerol-phosphate dehydratase, with EC number 4.2.1.19 Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of imidazoleglycerol-phosphate dehydratase., Glynn SE, Baker PJ, Sedelnikova SE, Davies CL, Eadsforth TC, Levy CW, Rodgers HF, Blackburn GM, Hawkes TR, Viner R, Rice DW, Structure. 2005 Dec;13(12):1809-17. PMID:16338409

Page seeded by OCA on Thu Feb 21 17:16:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2f1d.gif|left|200px]]<br /><applet load="2f1d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2f1d.gif|left|200px]]<br /><applet load="2f1d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2f1d, resolution 3.00&Aring;" />
 '''X-Ray Structure of imidazoleglycerol-phosphate dehydratase'''<br />
 ==Overview==
-The structure of A. thaliana imidazoleglycerol-phosphate dehydratase, an, enzyme of histidine biosynthesis and a target for the triazole phosphonate, herbicides, has been determined to 3.0 A resolution. The structure is, composed of 24 identical subunits arranged in 432 symmetry and shows how, the formation of a novel dimanganese cluster is crucial to the assembly of, the active 24-mer from an inactive trimeric precursor and to the formation, of the active site of the enzyme. Molecular modeling suggests that the, substrate is bound to the manganese cluster as an imidazolate moiety that, subsequently collapses to yield a diazafulvene intermediate. The mode of, imidazolate recognition exploits pseudosymmetry at the active site arising, from a combination of the assembly of the particle and the pseudosymmetry, present in each subunit as a result of gene duplication. This provides an, intriguing example of the role of evolution in the design of Nature's, catalysts.
+The structure of A. thaliana imidazoleglycerol-phosphate dehydratase, an enzyme of histidine biosynthesis and a target for the triazole phosphonate herbicides, has been determined to 3.0 A resolution. The structure is composed of 24 identical subunits arranged in 432 symmetry and shows how the formation of a novel dimanganese cluster is crucial to the assembly of the active 24-mer from an inactive trimeric precursor and to the formation of the active site of the enzyme. Molecular modeling suggests that the substrate is bound to the manganese cluster as an imidazolate moiety that subsequently collapses to yield a diazafulvene intermediate. The mode of imidazolate recognition exploits pseudosymmetry at the active site arising from a combination of the assembly of the particle and the pseudosymmetry present in each subunit as a result of gene duplication. This provides an intriguing example of the role of evolution in the design of Nature's catalysts.
 ==About this Structure==
-F1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with MN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Imidazoleglycerol-phosphate_dehydratase Imidazoleglycerol-phosphate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.19 4.2.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F1D OCA].
+F1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Imidazoleglycerol-phosphate_dehydratase Imidazoleglycerol-phosphate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.19 4.2.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F1D OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Imidazoleglycerol-phosphate dehydratase]]
 [[Category: Single protein]]
-[[Category: Baker, P.J.]]
+[[Category: Baker, P J.]]
-[[Category: Davies, C.L.]]
+[[Category: Davies, C L.]]
-[[Category: Eadsforth, T.C.]]
+[[Category: Eadsforth, T C.]]
-[[Category: Glynn, S.E.]]
+[[Category: Glynn, S E.]]
-[[Category: Rice, D.W.]]
+[[Category: Rice, D W.]]
-[[Category: Sedelnikova, S.E.]]
+[[Category: Sedelnikova, S E.]]
 [[Category: MN]]
 [[Category: SO4]]
@@ Line 28: / Line 28: @@
 [[Category: x-ray crystallography]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:17:58 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:42 2008''