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| [[Image:1rhy.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rhy| PDB=1rhy | SCENE= }} | | {{STRUCTURE_1rhy| PDB=1rhy | SCENE= }} |
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| '''Crystal structure of Imidazole Glycerol Phosphate Dehydratase'''
| | ===Crystal structure of Imidazole Glycerol Phosphate Dehydratase=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14724278}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14724278 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14724278}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Histidine biosynthesis]] | | [[Category: Histidine biosynthesis]] |
| [[Category: Left-handed b-a-b crossover motif]] | | [[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 Sun Jul 27 14:03:14 2008'' |
