2JWL

Solution Structure of periplasmic domain of TolR from H. influenzae with SAXS data

2JWL の概要

• エントリーDOI: 10.2210/pdb2jwl/pdb
• 関連するPDBエントリー: 2jwk
• 分子名称: Protein tolR (1 entity in total)
• 機能のキーワード: protein, periplasmic domain, membrane, inner membrane, protein transport, transmembrane, transport, membrane protein
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cell inner membrane; Single-pass type II membrane protein (By similarity): P43769
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16012.29

構造登録者

Parsons, L.M.,Bax, A.,Grishaev, A. (登録日: 2007-10-15, 公開日: 2008-04-01, 最終更新日: 2024-05-29)

主引用文献

Parsons, L.M.,Grishaev, A.,Bax, A.
The Periplasmic Domain of TolR from Haemophilus influenzae Forms a Dimer with a Large Hydrophobic Groove: NMR Solution Structure and Comparison to SAXS Data.
Biochemistry, 47:3131-3142, 2008

PubMed Abstract: TolR is a part of the Pal/Tol system which forms a five-member, membrane-spanning, multiprotein complex that is conserved in Gram-negative bacteria. The Pal/Tol system helps to maintain the integrity of the outer membrane and has been proposed to be involved in several other cellular processes including cell division. Obtaining the structure of TolR is of interest not only to help explain the many proposed functions of the Pal/Tol system but also to gain an understanding of the TolR homologues ExbD and MotB and to provide more targets for antibacterial treatments. In addition, the structure may provide insights into how colicins and bacteriophages are able to enter the cell. Here we report the solution structure of the homodimeric periplasmic domain of TolR from Haemophilus influenzae, determined with conventional, NOE-based NMR spectroscopy, supplemented by extensive residual dipolar coupling measurements. A novel method for assembling the dimer from small-angle X-ray scattering data confirms the NMR-derived structure. To facilitate NMR spectral analysis, a TolR construct containing residues 59-130 of the 139-residue protein was created. The periplasmic domain of TolR forms a C 2-symmetric dimer consisting of a strongly curved eight-stranded beta-sheet, generating a large deep groove on one side, while four helices cover the other face of the sheet. The structure of the TolR dimer together with data from the literature suggests how the periplasmic domain of TolR is most likely oriented relative to the cytoplasmic membrane and how it may interact with other components of the Pal/Tol system, particularly TolQ.

PubMed: 18269247
DOI: 10.1021/bi702283x

実験手法

SOLUTION NMR