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Structure and mechanism of imidazoleglycerol-phosphate dehydratase

Title: Structure and mechanism of imidazoleglycerol-phosphate dehydratase
Authors: Glynn, Steven E.; Baker, Patrick J.; Sedelnikova, Svetlana E.; Davies, Claire L.; Eadsforth, Thomas C.; Levy, Colin W.; Rodgers, H. Fiona; Blackburn, G. Michael; Hawkes, Timothy R.; Viner, Russell; Rice, David W.
Source: Glynn, S E, Baker, P J, Sedelnikova, S E, Davies, C L, Eadsforth, T C, Levy, C W, Rodgers, H F, Blackburn, G M, Hawkes, T R, Viner, R & Rice, D W 2005, 'Structure and mechanism of imidazoleglycerol-phosphate dehydratase', Structure, vol. 13, no. 12, pp. 1809-1817. https://doi.org/10.1016/j.str.2005.08.012
Publication Year: 2005
Collection: The University of Manchester: Research Explorer - Publications
Description: The structure of A. thaliana imidazoleglycerol-phosphate dehydratase, an enzyme of histidine biosynthesis and a target for the triazole phosphonate herbicides, has been determined to 3.0 Å resolution. The structure is composed of 24 identical subunits arranged in 432 symmetry and shows how the formation of a novel dimanganese cluster is crucial to the assembly of the active 24-mer from an inactive trimeric precursor and to the formation of the active site of the enzyme. Molecular modeling suggests that the substrate is bound to the manganese cluster as an imidazolate moiety that subsequently collapses to yield a diazafulvene intermediate. The mode of imidazolate recognition exploits pseudosymmetry at the active site arising from a combination of the assembly of the particle and the pseudosymmetry present in each subunit as a result of gene duplication. This provides an intriguing example of the role of evolution in the design of Nature's catalysts.
Document Type: article in journal/newspaper
Language: English
ISSN: 0969-2126; 1878-4186
Relation: info:eu-repo/semantics/altIdentifier/pmid/16338409; info:eu-repo/semantics/altIdentifier/pissn/0969-2126; info:eu-repo/semantics/altIdentifier/eissn/1878-4186
DOI: 10.1016/j.str.2005.08.012
Availability: https://research.manchester.ac.uk/en/publications/d3fdeeb5-15fe-4a73-9a84-65166510719d; https://doi.org/10.1016/j.str.2005.08.012; https://www.scopus.com/pages/publications/28844486198
Rights: info:eu-repo/semantics/openAccess
Accession Number: edsbas.1CC7268D
Database: BASE