2L26

Rv0899 from Mycobacterium tuberculosis contains two separated domains

Summary for 2L26

• Entry DOI: 10.2210/pdb2l26/pdb
• Descriptor: Uncharacterized protein Rv0899/MT0922 (1 entity in total)
• Functional Keywords: rv0899, out membrane protein, membrane protein
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cell membrane; Multi-pass membrane protein (Potential): P65593
• Total number of polymer chains: 1
• Total formula weight: 29443.13

Authors

Shi, C.,Li, J.,Gao, Y.,Wu, K.,Huang, H.,Tian, C. (deposition date: 2010-08-12, release date: 2011-08-17, Last modification date: 2024-10-16)

Primary citation

Li, J.,Shi, C.,Gao, Y.,Wu, K.,Shi, P.,Lai, C.,Chen, L.,Wu, F.,Tian, C.
Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal a Monomeric Membrane-Anchoring Protein with Two Separate Domains
J.Mol.Biol., 2011

PubMed Abstract: Rv0899 from Mycobacterium tuberculosis belongs to the OmpA (outer membrane protein A) family of outer membrane proteins. It functions as a pore-forming protein; the deletion of this gene impairs the uptake of some water-soluble substances, such as serine, glucose, and glycerol. Rv0899 has also been shown to play a part in low-pH environment adaption, which may play a part in pathogenic mycobacteria overcoming the host's defense mechanisms. Based on many bacterial physiological data and recent structural studies, it was proposed that Rv0899 forms an oligomeric channel to carry out such functions. In this work, biochemical and structural data obtained from solution NMR and EPR spectroscopy indicated that Rv0899 is a monomeric membrane-anchoring protein with two separate domains, rather than an oligomeric pore. Using NMR chemical shift perturbation and isothermal calorimetric titration assays, we show that Rv0899 was able to interact with Zn(2+) ions, which may indicate a role for Rv0899 in the process of Zn(2+) acquisition.

PubMed: 22108166
DOI: 10.1016/j.jmb.2011.11.016

Experimental method

SOLUTION NMR