2L26

Rv0899 from Mycobacterium tuberculosis contains two separated domains

2L26 の概要

• エントリーDOI: 10.2210/pdb2l26/pdb
• 分子名称: Uncharacterized protein Rv0899/MT0922 (1 entity in total)
• 機能のキーワード: rv0899, out membrane protein, membrane protein
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cell membrane; Multi-pass membrane protein (Potential): P65593
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29443.13

構造登録者

Shi, C.,Li, J.,Gao, Y.,Wu, K.,Huang, H.,Tian, C. (登録日: 2010-08-12, 公開日: 2011-08-17, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

SOLUTION NMR