1b1b

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spinqualitylabelsall models 1b1b, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

IRON DEPENDENT REGULATOR

Overview

Iron-dependent regulators are a family of metal-activated DNA binding, proteins found in several Gram-positive bacteria. These proteins are, negative regulators of virulence factors and of proteins of bacterial, iron-uptake systems. In this study we present the crystal structure of the, iron-dependent regulator (IdeR) from Mycobacterium tuberculosis, the, causative agent of tuberculosis. The protein crystallizes in the hexagonal, space group P62 with unit cell dimensions a=b=92.6 A, c=63.2 A. The, current model comprises the N-terminal DNA-binding domain (residues 1-73), and the dimerization domain (residues 74-140), while the third domain, (residues 141-230) is too disordered to be included. The molecule lies on, a crystallographic 2-fold axis that generates the functional dimer. The, overall structure of the monomer shares many features with the homologous, regulator, diphtheria toxin repressor (DtxR) from Corynebacterium, diphtheriae. The IdeR structure in complex with Zinc reported here is, however, the first wild-type repressor structure with both metal binding, sites fully occupied. This crystal structure reveals that both Met10 and, most probably the Sgamma of Cys102 are ligands of the second metal binding, site. In addition, there are important changes in the tertiary structure, between apo-DtxR and holo-IdeR bringing the putative DNA binding helices, closer together in the holo repressor. The mechanism by which metal, binding may cause these structural changes between apo and holo wild-type, repressor is discussed.

About this Structure

1B1B is a Single protein structure of sequence from Mycobacterium tuberculosis with ZN and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied., Pohl E, Holmes RK, Hol WG, J Mol Biol. 1999 Jan 22;285(3):1145-56. PMID:9887269

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