1zud

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models PDB ID 1zud Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.98Å
Ligands:	, and
Coordinates:	save as pdb, mmCIF, xml

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. 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 Thu Mar 20 15:39:55 2008