1zud
From Proteopedia
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Structure of ThiS-ThiF protein complex
Overview
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, donor for thiazole formation. ThiS is a small 7.2 kDa protein that, structurally resembles ubiquitin and the molybdopterin biosynthetic, protein MoaD. ThiF is a 27 kDa protein with distinct sequence and, structural similarity to the ubiquitin activating enzyme E1 and the, molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies, the mechanism of the sulfur transfer chemistry involved in thiazole, biosynthesis.
About this Structure
1ZUD is a Protein complex structure of sequences from Escherichia coli with ZN, CA and NA as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis., Lehmann C, Begley TP, Ealick SE, Biochemistry. 2006 Jan 10;45(1):11-9. PMID:16388576
Page seeded by OCA on Wed Nov 21 07:39:56 2007
Categories: Escherichia coli | Protein complex | Ealick, S.E. | Lehmann, C. | CA | NA | ZN | Protein-protein complex | Thiamin | Thiazole | Thif | This
