1fx7

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1fx7, resolution 2.00Å

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CRYSTAL STRUCTURE OF THE IRON-DEPENDENT REGULATOR (IDER) FROM MYCOBACTERIUM TUBERCULOSIS

Overview

Iron-dependent regulators are primary transcriptional regulators of, virulence factors and iron scavenging systems that are important for, infection by several bacterial pathogens. Here we present the 2.0-A, crystal structure of the wild type iron-dependent regulator from, Mycobacterium tuberculosis in its fully active holorepressor conformation., Clear, unbiased electron density for the Src homology domain 3-like third, domain, which is often invisible in structures of iron-dependent, regulators, was revealed by density modification and averaging. This, domain is one of the rare examples of Src homology domain 3-like folds in, bacterial proteins, and, in addition, displays a metal binding function by, contributing two ligands, one Glu and one Gln, to the pentacoordinated, cobalt atom at metal site 1. Both metal sites are fully occupied, and, tightly bound water molecules at metal site 1 ("Water 1") and metal site 2, ("Water 2") are identified unambiguously. The main chain carbonyl of Leu4, makes an indirect interaction with the cobalt atom at metal site 2 via, Water 2, and the adjacent residue, Val5, forms a rare gamma turn. Residues, 1-3 are well ordered and make numerous interactions. These ordered solvent, molecules and the conformation and interactions of the N-terminal, pentapeptide thus might be important in metal-dependent activation.

About this Structure

1FX7 is a Single protein structure of sequence from Mycobacterium tuberculosis with SO4 and CO as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain., Feese MD, Ingason BP, Goranson-Siekierke J, Holmes RK, Hol WG, J Biol Chem. 2001 Feb 23;276(8):5959-66. Epub 2000 Oct 26. PMID:11053439

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