Advertisement

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Biological Chemistry

Mycobacteria Have A System For Acquiring Iron From Heme …

In addition to using iron-chelating siderophores, the tuberculosis microbe uses a heme-binding protein to grab iron

by Celia Henry Arnaud
March 14, 2011 | A version of this story appeared in Volume 89, Issue 11

[+]Enlarge
Credit: Proc. Natl. Acad. Sci. USA
The tetrameric Rv0203 heme-binding protein.
Credit: Proc. Natl. Acad. Sci. USA
The tetrameric Rv0203 heme-binding protein.

The tuberculosis-causing microorganism, Mycobacterium tuberculosis, has a system for acquiring iron from free heme and hemoglobin, molecular biologists have discovered (Proc. Natl. Acad. Sci. USA, DOI: 10.1073/pnas.1009516108). This system could provide a new target for tuberculosis therapeutics. Until recently, M. tuberculosis, which usually gets its iron by using molecules called siderophores to remove the metal from the human proteins transferrin and lactoferrin, seemed unable to use the more abundant iron bound by heme and hemoglobin. But Celia W. Goulding of the University of California, Irvine, and coworkers have now found and characterized a mycobacterial heme acquisition system. Using affinity chromatography, the researchers captured the heme-binding protein Rv0203. They solved the crystal structure of the protein, which is a dimer of dimers. Each monomer consists of five α-helices, and the dimers form a cagelike structure with a hydrophobic core. The key residues in the heme-binding site are two histidines and a tyrosine. In addition, Goulding and coworkers identified two putative transmembrane heme transporters in the microorganism.

Article:

This article has been sent to the following recipient:

0 /1 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.