title: Structural studies of Mycobacterium tuberculosis Rv0899 reveal a monomeric membrane-anchoring protein with two separate domains.
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.
authors: Hefei National Laboratory for Physical Science at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230027, China.
authors: Juan
authors: J
authors: Li
authors: Chaowei
authors: C
authors: Shi
authors: Yuan
authors: Y
authors: Gao
authors: Kaiqi
authors: K
authors: Wu
authors: Pan
authors: P
authors: Shi
authors: Chaohua
authors: C
authors: Lai
authors: Liu
authors: L
authors: Chen
authors: Fangming
authors: F
authors: Wu
authors: Changlin
authors: C
authors: Tian
mesh_terms: D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D002151:Calorimetry; D002413:Cations, Divalent / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D009682:Magnetic Resonance Spectroscopy; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D015032:Zinc / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D002413:Cations, Divalent; D015032:Zinc