|PROSITE documentation PDOC00581 [for PROSITE entry PS51177]|
Riboflavin synthase (RS-α) catalyzes the biosynthesis of riboflavin (vitamin B2) by dismutation of 6,7-dimethyl-8-(1'-D-ribityl)lumazine (Lum) (EC 188.8.131.52). Riboflavin synthases of bacteria and fungi are structurally and evolutionary related to antenna proteins involved in bioluminescence of marine bacteria [1,2]. These proteins seem to have evolved from the duplication of a domain of about 100 residues, the lumazine-binding repeat.
The 3D structure of RS-α, which is an asymmetric homotrimer, shows that both domains form a 6-stranded antiparallel β-barrel (see <PDB:1PKV>) , while a C-terminal helix is involved in trimerization. The Lum-binding domain of RS-α forms two Greek-key folds with the topology BBHBBBHB, where most of the substrate binding sites are located in β-strands (B) 4 and 5 and in helix (H) 2 [3,4,5].
Some proteins known to contain a lumazine-binding repeat:
The profile we developed covers the entire lumazine-binding repeat.Last update:
December 2005 / Pattern removed, profile added and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||O'Kane D.J. Woodward B. Lee J. Prasher D.C.|
|Title||Borrowed proteins in bacterial bioluminescence.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 88:1100-1104(1991).|
|2||Authors||O'Kane D.J. Prasher D.C.|
|Title||Evolutionary origins of bacterial bioluminescence.|
|Source||Mol. Microbiol. 6:443-449(1992).|
|3||Authors||Meining W. Eberhardt S. Bacher A. Ladenstein R.|
|Title||The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution.|
|Source||J. Mol. Biol. 331:1053-1063(2003).|
|4||Authors||Truffault V. Coles M. Diercks T. Abelmann K. Eberhardt S. Luttgen H. Bacher A. Kessler H.|
|Title||The solution structure of the N-terminal domain of riboflavin synthase.|
|Source||J. Mol. Biol. 309:949-960(2001).|
|5||Authors||Gerhardt S. Schott A.K. Kairies N. Cushman M. Illarionov B. Eisenreich W. Bacher A. Huber R. Steinbacher S. Fischer M.|
|Title||Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine.|