3TUI

Inward facing conformations of the MetNI methionine ABC transporter: CY5 native crystal form

3TUI の概要

• エントリーDOI: 10.2210/pdb3tui/pdb
• 関連するPDBエントリー: 3DHW 3DHX
• 分子名称: D-methionine transport system permease protein metI, Methionine import ATP-binding protein MetN, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: abc-transporter, type i abc type importer, methionine uptake transporter, membrane protein, amino-acid transport, atp-binding, hydrolase, inner membrane, hydrolase-transport protein complex, hydrolase/transport protein
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P31547; Cell inner membrane; Peripheral membrane protein (By similarity): P30750
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 257229.36

構造登録者

Johnson, E.,Nguyen, P.T.,Rees, D.C. (登録日: 2011-09-16, 公開日: 2011-11-30, 最終更新日: 2023-09-13)

主引用文献

Johnson, E.,Nguyen, P.T.,Yeates, T.O.,Rees, D.C.
Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition.
Protein Sci., 21:84-96, 2012

PubMed Abstract: Two new crystal structures of the Escherichia coli high affinity methionine uptake ATP Binding Cassette (ABC) transporter MetNI, purified in the detergents cyclohexyl-pentyl-β-D-maltoside (CY5) and n-decyl-β-D-maltopyranoside (DM), have been solved in inward facing conformations to resolutions of 2.9 and 4.0 Å, respectively. Compared to the previously reported 3.7 Å resolution structure of MetNI purified in n-dodecyl-β-D-maltopyranoside (DDM), the higher resolution of the CY5 data enabled significant improvements to the structural model in several regions, including corrections to the sequence registry, and identification of ADP in the nucleotide binding site. CY5 crystals soaked with selenomethionine established details of the methionine binding site in the C2 regulatory domain of the ABC subunit, including the displacement of the side chain of MetN residue methionine 301 by the exogenous ligand. When compared to the CY5 or DDM structures, the DM structure exhibits a significant repositioning of the dimeric C2 domains, including an unexpected register shift in the intermolecular β-sheet hydrogen bonding between monomers, and a narrowing of the nucleotide binding space. The immediate proximity of the exogenous methionine binding site to the conformationally variable dimeric interface provides an indication of how methionine binding to the regulatory domains might mediate the phenomenon of transinhibition.

PubMed: 22095702
DOI: 10.1002/pro.765

実験手法

X-RAY DIFFRACTION (2.9 Å)