1rhy
From Proteopedia
(New page: 200px<br /><applet load="1rhy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhy, resolution 2.30Å" /> '''Crystal structure of...) |
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- | [[Image:1rhy.gif|left|200px]]<br /><applet load="1rhy" size=" | + | [[Image:1rhy.gif|left|200px]]<br /><applet load="1rhy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rhy, resolution 2.30Å" /> | caption="1rhy, resolution 2.30Å" /> | ||
'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase'''<br /> | '''Crystal structure of Imidazole Glycerol Phosphate Dehydratase'''<br /> | ||
==Overview== | ==Overview== | ||
- | Imidazole glycerol-phosphate dehydratase (IGPD) catalyzes the sixth step | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Burgner, J | + | [[Category: Burgner, J W.]] |
- | [[Category: Chaudhuri, B | + | [[Category: Chaudhuri, B N.]] |
- | [[Category: Davisson, V | + | [[Category: Davisson, V J.]] |
- | [[Category: Sinha, S | + | [[Category: Sinha, S C.]] |
- | [[Category: Smith, J | + | [[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]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 14:51:04 2008
Categories: Filobasidiella neoformans | Imidazoleglycerol-phosphate dehydratase | Single protein | Burgner, J W. | Chaudhuri, B N. | Davisson, V J. | Sinha, S C. | Smith, J L. | Yakovleva, G. | ACY | EMC | GOL | HG | SO4 | Dehydratases; histidine biosynthesis; left-handed b-a-b crossover motif; gene duplication