Abstract:
:Riboflavin synthase is a trimer of identical 23-kDa subunits. The primary structure is characterized by considerable similarity of the C-terminal and N-terminal parts. Recombinant riboflavin synthase of Escherichia coli and Bacillus subtilis was crystallized by the vapor diffusion method. Crystals of E. coli riboflavin synthase belong to the orthorhombic system, space group P2(1)2(1)2(1), with unit cell dimensions a = 53.2 A, b = 117.6 A, c = 150.9 A, alpha = beta = gamma = 90 degrees. They diffract to better than 3.3 A resolution and have presumably one trimer in the asymmetric unit. The self rotation function indicates local 32 symmetry. Twofold local symmetry is an unexpected result in a trimeric protein. In conjunction with primary structure arguments and mechanistic considerations, we propose that the protein is a pseudohexamer where each of the peptide subunits fold into two topologically similar domains.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Meining W,Tibbelin G,Ladenstein R,Eberhardt S,Fischer M,Bacher Adoi
10.1006/jsbi.1997.3935subject
Has Abstractpub_date
1998-01-01 00:00:00pages
53-60issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(97)93935-6journal_volume
121pub_type
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