Crystal Structure of an Archaeal Pentameric Riboflavin Synthase in Complex with a Substrate Analog Inhibitor: Stereochemical Implications.
From: Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, Martinsried, Germany. ramsperg@biochem.mpg.de
The Journal of biological chemistry
- Publish Date: Jan 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 2
- Pages: 1224-32
- Medium: Print
- Language: English
- Citation (JAMA): Ramsperger Arne, Augustin Martin, Schott Ann-Kathrin, et al. Crystal Structure of an Archaeal Pentameric Riboflavin Synthase in Complex with a Substrate Analog Inhibitor: Stereochemical Implications.. J. Biol. Chem. Jan 2006;281:1224-32
Abstract
Whereas eubacterial and eukaryotic riboflavin synthases form homotrimers, archaeal riboflavin synthases from Methanocaldococcus jannaschii and Methanothermobacter thermoautrophicus are homopentamers with sequence similarity to the 6,7-dimethyl-8-ribityllumazine synthase catalyzing the penultimate step in riboflavin biosynthesis. Recently it could be shown that the complex dismutation reaction catalyzed by the pentameric M. jannaschii riboflavin synthase generates riboflavin with the same regiochemistry as observed for trimeric riboflavin synthases. Here we present crystal structures of the pentameric riboflavin synthase from M. jannaschii and its complex with the substrate analog inhibitor, 6,7-dioxo-8-ribityllumazine. The complex structure shows five active sites located between adjacent monomers of the pentamer. Each active site can accommodate two substrate analog molecules in anti-parallel orientation. The topology of the two bound ligands at the active site is well in line with the known stereochemistry of a pentacyclic adduct of 6,7-dimethyl-8-ribityllumazine that has been shown to serve as a kinetically competent intermediate. The pentacyclic intermediates of trimeric and pentameric riboflavin synthases are diastereomers.
Mesh Headings (Keywords): Amino Acid Sequence, Archaea, Binding Sites, Cloning, Molecular, Crystallography, X-Ray, Kinetics, Methanobacteriaceae, Models, Chemical, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Multienzyme Complexes, Protein Conformation, Protein Structure, Secondary, Pteridines, Ribitol, Riboflavin, Riboflavin Synthase, Ribose, Sequence Homology, Amino Acid, Stereoisomerism
Check for Full Text / PubMed Unique Identifier (PMID): 16272154
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