1rhy: Difference between revisions
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'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase''' | {{Structure | ||
|PDB= 1rhy |SIZE=350|CAPTION= <scene name='initialview01'>1rhy</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [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] | |||
|GENE= HIS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5207 Filobasidiella neoformans]) | |||
}} | |||
'''Crystal structure of Imidazole Glycerol Phosphate Dehydratase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RHY is a [ | 1RHY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Filobasidiella_neoformans Filobasidiella neoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14724278 14724278] | ||
[[Category: Filobasidiella neoformans]] | [[Category: Filobasidiella neoformans]] | ||
[[Category: Imidazoleglycerol-phosphate dehydratase]] | [[Category: Imidazoleglycerol-phosphate dehydratase]] | ||
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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://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:52 2008'' | ||
Revision as of 11:51, 20 March 2008
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| 1rhy, resolution 2.30Å | |||||||||||||
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| Ligands: | HG, EMC, SO4, ACY and GOL | ||||||||||||
| Gene: | HIS3 (Filobasidiella neoformans) | ||||||||||||
| Activity: | Imidazoleglycerol-phosphate dehydratase, with EC number 4.2.1.19 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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