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1rhy
From Proteopedia
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'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase''' | '''Crystal structure of Imidazole Glycerol Phosphate Dehydratase''' | ||
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[[Category: Smith, J L.]] | [[Category: Smith, J L.]] | ||
[[Category: Yakovleva, G.]] | [[Category: Yakovleva, G.]] | ||
| - | [[Category: | + | [[Category: Dehydratase]] |
| - | [[Category: | + | [[Category: Gene duplication]] |
| - | [[Category: | + | [[Category: Histidine biosynthesis]] |
| - | [[Category: | + | [[Category: Left-handed b-a-b crossover motif]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:31:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:31, 3 May 2008
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. 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 Sat May 3 07:31:03 2008
