Ontology highlight
ABSTRACT:
SUBMITTER: Lehmann C
PROVIDER: S-EPMC2566941 | biostudies-literature | 2006 Jan
REPOSITORIES: biostudies-literature
Lehmann Christopher C Begley Tadhg P TP Ealick Steven E SE
Biochemistry 20060101 1
We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur ...[more]