1rhy

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(New page: 200px<br /><applet load="1rhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhy, resolution 2.30&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase'''<br />
'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase'''<br />
==Overview==
==Overview==
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Imidazole glycerol-phosphate dehydratase (IGPD) catalyzes the sixth step, of histidine biosynthesis. The enzyme is of fundamental biochemical, interest, because it catalyzes removal of a non-acidic hydrogen atom in, the dehydration reaction. It is also a potential target for development of, herbicides. IGPD is a metalloenzyme in which transition metals induce, aggregation and are required for catalysis. Addition of 1 equivalent of, Mn(2+)/subunit is shown by analytical ultracentrifugation to induce the, formation of 24-mers from trimeric IGPD. Two histidine-rich motifs may, participate in metal binding and aggregation. The 2.3-A crystal structure, of metal-free trimeric IGPD from the fungus Filobasidiella neoformans, reveals a novel fold containing an internal repeat, apparently the result, of gene duplication. The 95-residue alpha/beta half-domain occurs in a few, other proteins, including the GHMP kinase superfamily, (galacto-homoserine-mevalonate-phosphomevalonate), but duplication to form, a compact domain has not been seen elsewhere. Conserved residues cluster, at two types of sites in the trimer, each site containing a conserved, histidine-rich motif. A model is proposed for the intact, active 24-mer in, which all highly conserved residues, including the histidine-rich motifs, in both the N- and C-terminal halves of the polypeptide, cluster at a, common site between trimers. This site is a candidate for the active site, and also for metal binding leading to aggregation of trimers. The, structure provides a basis for further studies of enzyme function and, mechanism and for development of more potent and specific herbicides.
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Imidazole glycerol-phosphate dehydratase (IGPD) catalyzes the sixth step of histidine biosynthesis. The enzyme is of fundamental biochemical interest, because it catalyzes removal of a non-acidic hydrogen atom in the dehydration reaction. It is also a potential target for development of herbicides. IGPD is a metalloenzyme in which transition metals induce aggregation and are required for catalysis. Addition of 1 equivalent of Mn(2+)/subunit is shown by analytical ultracentrifugation to induce the formation of 24-mers from trimeric IGPD. Two histidine-rich motifs may participate in metal binding and aggregation. The 2.3-A crystal structure of metal-free trimeric IGPD from the fungus Filobasidiella neoformans reveals a novel fold containing an internal repeat, apparently the result of gene duplication. The 95-residue alpha/beta half-domain occurs in a few other proteins, including the GHMP kinase superfamily (galacto-homoserine-mevalonate-phosphomevalonate), but duplication to form a compact domain has not been seen elsewhere. Conserved residues cluster at two types of sites in the trimer, each site containing a conserved histidine-rich motif. A model is proposed for the intact, active 24-mer in which all highly conserved residues, including the histidine-rich motifs in both the N- and C-terminal halves of the polypeptide, cluster at a common site between trimers. This site is a candidate for the active site and also for metal binding leading to aggregation of trimers. The structure provides a basis for further studies of enzyme function and mechanism and for development of more potent and specific herbicides.
==About this Structure==
==About this Structure==
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1RHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Filobasidiella_neoformans Filobasidiella neoformans] with HG, EMC, SO4, ACY and GOL 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=1RHY OCA].
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1RHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Filobasidiella_neoformans Filobasidiella neoformans] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=EMC:'>EMC</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=GOL:'>GOL</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=1RHY OCA].
==Reference==
==Reference==
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[[Category: Imidazoleglycerol-phosphate dehydratase]]
[[Category: Imidazoleglycerol-phosphate dehydratase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Burgner, J.W.]]
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[[Category: Burgner, J W.]]
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[[Category: Chaudhuri, B.N.]]
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[[Category: Chaudhuri, B N.]]
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[[Category: Davisson, V.J.]]
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[[Category: Davisson, V J.]]
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[[Category: Sinha, S.C.]]
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[[Category: Sinha, S C.]]
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[[Category: Smith, J.L.]]
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[[Category: Smith, J L.]]
[[Category: Yakovleva, G.]]
[[Category: Yakovleva, G.]]
[[Category: ACY]]
[[Category: ACY]]
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[[Category: dehydratases; histidine biosynthesis; left-handed b-a-b crossover motif; gene duplication]]
[[Category: dehydratases; histidine biosynthesis; left-handed b-a-b crossover motif; gene duplication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:04 2008''

Revision as of 12:51, 21 February 2008


1rhy, resolution 2.30Å

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Crystal structure of Imidazole Glycerol Phosphate Dehydratase

Overview

Imidazole glycerol-phosphate dehydratase (IGPD) catalyzes the sixth step of histidine biosynthesis. The enzyme is of fundamental biochemical interest, because it catalyzes removal of a non-acidic hydrogen atom in the dehydration reaction. It is also a potential target for development of herbicides. IGPD is a metalloenzyme in which transition metals induce aggregation and are required for catalysis. Addition of 1 equivalent of Mn(2+)/subunit is shown by analytical ultracentrifugation to induce the formation of 24-mers from trimeric IGPD. Two histidine-rich motifs may participate in metal binding and aggregation. The 2.3-A crystal structure of metal-free trimeric IGPD from the fungus Filobasidiella neoformans reveals a novel fold containing an internal repeat, apparently the result of gene duplication. The 95-residue alpha/beta half-domain occurs in a few other proteins, including the GHMP kinase superfamily (galacto-homoserine-mevalonate-phosphomevalonate), but duplication to form a compact domain has not been seen elsewhere. Conserved residues cluster at two types of sites in the trimer, each site containing a conserved histidine-rich motif. A model is proposed for the intact, active 24-mer in which all highly conserved residues, including the histidine-rich motifs in both the N- and C-terminal halves of the polypeptide, cluster at a common site between trimers. This site is a candidate for the active site and also for metal binding leading to aggregation of trimers. The structure provides a basis for further studies of enzyme function and mechanism and for development of more potent and specific herbicides.

About this Structure

1RHY is a Single protein structure of sequence from Filobasidiella neoformans with , , , and as ligands. Active as Imidazoleglycerol-phosphate dehydratase, with EC number 4.2.1.19 Full crystallographic information is available from OCA.

Reference

Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold., Sinha SC, Chaudhuri BN, Burgner JW, Yakovleva G, Davisson VJ, Smith JL, J Biol Chem. 2004 Apr 9;279(15):15491-8. Epub 2004 Jan 14. PMID:14724278

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