3FVQ

Crystal structure of the nucleotide binding domain FbpC complexed with ATP

3FVQ の概要

• エントリーDOI: 10.2210/pdb3fvq/pdb
• 分子名称: Fe(3+) ions import ATP-binding protein fbpC, ADENOSINE-5'-TRIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: nucleotide binding domain, abc motor domain, ferric iron transport, atp-binding, cell inner membrane, cell membrane, hydrolase, ion transport, iron, iron transport, membrane, nucleotide-binding, transport
• 由来する生物種: Neisseria gonorrhoeae
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein (By similarity): Q5FA19
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78921.03

構造登録者

Newstead, S.,Bilton, P.,Carpenter, E.P.,Campopiano, D.,Iwata, S. (登録日: 2009-01-16, 公開日: 2009-08-25, 最終更新日: 2024-02-21)

主引用文献

Newstead, S.,Fowler, P.W.,Bilton, P.,Carpenter, E.P.,Sadler, P.J.,Campopiano, D.J.,Sansom, M.S.,Iwata, S.
Insights into how nucleotide-binding domains power ABC transport.
Structure, 17:1213-1222, 2009

PubMed Abstract: The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters power the transport of substrates across cell membranes is currently unclear. Here we report the crystal structure of an NBD, FbpC, from the Neisseria gonorrhoeae ferric iron uptake transporter with an unusual and substantial domain swap in the C-terminal regulatory domain. This entanglement suggests that FbpC is unable to open to the same extent as the homologous protein MalK. Using molecular dynamics we demonstrate that this is not the case: both NBDs open rapidly once ATP is removed. We conclude from this result that the closed structures of FbpC and MalK have higher free energies than their respective open states. This result has important implications for our understanding of the mechanism of power generation in ABC transporters, because the unwinding of this free energy ensures that the opening of these two NBDs is also powered.

PubMed: 19748342
DOI: 10.1016/j.str.2009.07.009

実験手法

X-RAY DIFFRACTION (1.9 Å)