4K7K

Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation

4K7K の概要

• エントリーDOI: 10.2210/pdb4k7k/pdb
• 分子名称: Cation efflux system protein CusC (2 entities in total)
• 機能のキーワード: beta barrel, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P77211
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 98783.95

構造登録者

Su, C.-C.,Lei, H.-T. (登録日: 2013-04-17, 公開日: 2013-10-16, 最終更新日: 2024-02-28)

主引用文献

Lei, H.T.,Bolla, J.R.,Bishop, N.R.,Su, C.C.,Yu, E.W.
Crystal Structures of CusC Review Conformational Changes Accompanying Folding and Transmembrane Channel Formation.
J.Mol.Biol., 426:403-411, 2014

PubMed Abstract: Gram-negative bacteria, such as Escherichia coli, frequently utilize tripartite efflux complexes in the RND (resistance-nodulation-cell division) family to expel diverse toxic compounds from the cell. These complexes span both the inner and outer membranes of the bacterium via an α-helical, inner membrane transporter; a periplasmic membrane fusion protein; and a β-barrel, outer membrane channel. One such efflux system, CusCBA, is responsible for extruding biocidal Cu(I) and Ag(I) ions. To remove these toxic ions, the CusC outer membrane channel must form a β-barrel structural domain, which creates a pore and spans the entire outer membrane. We here report the crystal structures of wild-type CusC, as well as two CusC mutants, suggesting that the first N-terminal cysteine residue plays an important role in protein-membrane interactions and is critical for the insertion of this channel protein into the outer membrane. These structures provide insight into the mechanisms on CusC folding and transmembrane channel formation. It is found that the interactions between CusC and membrane may be crucial for controlling the opening and closing of this β-barrel, outer membrane channel.

PubMed: 24099674
DOI: 10.1016/j.jmb.2013.09.042

実験手法

X-RAY DIFFRACTION (2.53 Å)