1nqw
From Proteopedia
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'''Crystal Structure of Lumazine Synthase from Aquifex aeolicus in Complex with Inhibitor: 5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid''' | '''Crystal Structure of Lumazine Synthase from Aquifex aeolicus in Complex with Inhibitor: 5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid''' | ||
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[[Category: Meining, W.]] | [[Category: Meining, W.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
| - | [[Category: | + | [[Category: Aquifex aeolicus]] |
| - | [[Category: | + | [[Category: Catalytic mechanism]] |
| - | [[Category: | + | [[Category: Inhibitor complex]] |
| - | [[Category: | + | [[Category: Lumazine synthase]] |
| - | [[Category: | + | [[Category: Vitamin biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:52:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:52, 2 May 2008
Crystal Structure of Lumazine Synthase from Aquifex aeolicus in Complex with Inhibitor: 5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid
Overview
6,7-Dimethyl-8-ribityllumazine is the biosynthetic precursor of riboflavin, which, as a coenzyme, plays a vital role in the electron transfer process for energy production in all cellular organisms. The enzymes involved in lumazine biosynthesis have been studied in considerable detail. However, the conclusive mechanism of the reaction catalyzed by lumazine synthase has remained unclear. Here, we report four crystal structures of the enzyme from the hyperthermophilic bacterium Aquifex aeolicus in complex with different inhibitor compounds. The structures were refined at resolutions of 1.72 A, 1.85 A, 2.05 A and 2.2 A, respectively. The inhibitors have been designed in order to mimic the substrate, the putative reaction intermediates and the final product. Structural comparisons of the native enzyme and the inhibitor complexes as well as the kinetic data of single-site mutants of lumazine synthase from Bacillus subtilis showed that several highly conserved residues at the active site, namely Phe22, His88, Arg127, Lys135 and Glu138 are most likely involved in catalysis. A structural model of the catalytic process, which illustrates binding of substrates, enantiomer specificity, proton abstraction/donation, inorganic phosphate elimination, formation of the Schiff base and cyclization is proposed.
About this Structure
1NQW is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
A structure-based model of the reaction catalyzed by lumazine synthase from Aquifex aeolicus., Zhang X, Meining W, Cushman M, Haase I, Fischer M, Bacher A, Ladenstein R, J Mol Biol. 2003 Apr 18;328(1):167-82. PMID:12684006 Page seeded by OCA on Sat May 3 02:52:26 2008
