4Q7M

Structure of NBD288-Avi of TM287/288

4Q7M の概要

• エントリーDOI: 10.2210/pdb4q7m/pdb
• 関連するPDBエントリー: 3QF4 4Q7K 4Q7L
• 分子名称: Uncharacterized ABC transporter ATP-binding protein TM_0288 (2 entities in total)
• 機能のキーワード: abc-type nucleotide binding domain (nbd), metal binding protein
• 由来する生物種: Thermotoga maritima
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q9WYC4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30691.26

構造登録者

Bukowska, M.A.,Hohl, M.,Gruetter, M.G.,Seeger, M.A. (登録日: 2014-04-25, 公開日: 2015-05-20, 最終更新日: 2024-02-28)

主引用文献

Bukowska, M.A.,Hohl, M.,Geertsma, E.R.,Hurlimann, L.M.,Grutter, M.G.,Seeger, M.A.
A Transporter Motor Taken Apart: Flexibility in the Nucleotide Binding Domains of a Heterodimeric ABC Exporter.
Biochemistry, 54:3086-3099, 2015

PubMed Abstract: ABC exporters are ubiquitous multidomain transport proteins that couple ATP hydrolysis at a pair of nucleotide binding domains to substrate transport across the lipid bilayer mediated by two transmembrane domains. Recently, the crystal structure of the heterodimeric ABC exporter TM287/288 was determined. One of its asymmetric ATP binding sites is called the degenerate site; it binds nucleotides tightly but is impaired in terms of ATP hydrolysis. Here we report the crystal structures of both isolated motor domains of TM287/288. Unexpectedly, structural elements constituting the degenerate ATP binding site are disordered in these crystals and become structured only in the context of the full-length transporter. In addition, hydrogen bonding patterns of key residues, including those of the catalytically important Walker B and the switch loop motifs, are fundamentally different in the solitary NBDs compared to those in the intact transport protein. The structures reveal crucial interdomain contacts that need to be established for the proper assembly of the functional transporter complex.

PubMed: 25947941
DOI: 10.1021/acs.biochem.5b00188

実験手法

X-RAY DIFFRACTION (2.3 Å)