1N2Z

2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli

1N2Z の概要

• エントリーDOI: 10.2210/pdb1n2z/pdb
• 分子名称: Vitamin B12 transport protein btuF, CADMIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P37028
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59686.36

構造登録者

Borths, E.L.,Locher, K.P.,Lee, A.T.,Rees, D.C. (登録日: 2002-10-24, 公開日: 2002-12-18, 最終更新日: 2024-10-09)

主引用文献

Borths, E.L.,Locher, K.P.,Lee, A.T.,Rees, D.C.
The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
Proc.Natl.Acad.Sci.USA, 99:16642-16647, 2002

PubMed Abstract: Bacterial binding protein-dependent ATP binding cassette (ABC) transporters facilitate uptake of essential nutrients. The crystal structure of Escherichia coli BtuF, the protein that binds vitamin B12 and delivers it to the periplasmic surface of the ABC transporter BtuCD, reveals a bi-lobed fold resembling that of the ferrichrome binding protein FhuD. B12 is bound in the "base-on" conformation in a deep cleft formed at the interface between the two lobes of BtuF. A stable complex between BtuF and BtuCD (with the stoichiometry BtuC2D2F) is demonstrated to form in vitro and was modeled using the individual crystal structures. Two surface glutamates from BtuF may interact with arginine residues on the periplasmic surface of the BtuCD transporter. These glutamate and arginine residues are conserved among binding proteins and ABC transporters mediating iron and B12 uptake, suggesting that they may have a role in docking and the transmission of conformational changes.

PubMed: 12475936
DOI: 10.1073/pnas.262659699

実験手法

X-RAY DIFFRACTION (2 Å)