3MAY

Crystal structure of a secreted Mycobacterium tuberculosis heme-binding protein

Summary for 3MAY

• Entry DOI: 10.2210/pdb3may/pdb
• Descriptor: POSSIBLE EXPORTED PROTEIN (2 entities in total)
• Functional Keywords: helical protein, heme-binding protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 8
• Total formula weight: 83277.74

Authors

Goulding, C.W.,Chim, N. (deposition date: 2010-03-24, release date: 2011-03-23, Last modification date: 2011-07-13)

Primary citation

Tullius, M.V.,Harmston, C.A.,Owens, C.P.,Chim, N.,Morse, R.P.,McMath, L.M.,Iniguez, A.,Kimmey, J.M.,Sawaya, M.R.,Whitelegge, J.P.,Horwitz, M.A.,Goulding, C.W.
Discovery and characterization of a unique mycobacterial heme acquisition system.
Proc.Natl.Acad.Sci.USA, 108:5051-5056, 2011

PubMed Abstract: Mycobacterium tuberculosis must import iron from its host for survival, and its siderophore-dependent iron acquisition pathways are well established. Here we demonstrate a newly characterized pathway, whereby M. tuberculosis can use free heme and heme from hemoglobin as an iron source. Significantly, we identified the genomic region, Rv0202c-Rv0207c, responsible for the passage of heme iron across the mycobacterial membrane. Key players of this heme uptake system were characterized including a secreted protein and two transmembrane proteins, all three specific to mycobacteria. Furthermore, the crystal structure of the key heme carrier protein Rv0203 was found to have a unique fold. The discovery of a unique mycobacterial heme acquisition pathway opens new avenues of exploration into mycobacterial therapeutics.

PubMed: 21383189
DOI: 10.1073/pnas.1009516108

Experimental method

X-RAY DIFFRACTION (2.5 Å)