Evidence for local 32 symmetry in homotrimeric riboflavin synthase of Escherichia coli.

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 Biol

authors

Meining W,Tibbelin G,Ladenstein R,Eberhardt S,Fischer M,Bacher A

doi

10.1006/jsbi.1997.3935

subject

Has Abstract

pub_date

1998-01-01 00:00:00

pages

53-60

issue

1

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(97)93935-6

journal_volume

121

pub_type

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