1UYO

Translocator domain of autotransporter NalP from Neisseria meningitidis

1UYO の概要

• エントリーDOI: 10.2210/pdb1uyo/pdb
• 関連するPDBエントリー: 1UYN
• 分子名称: NALP, PENTAETHYLENE GLYCOL MONODECYL ETHER (2 entities in total)
• 機能のキーワード: autotransporter, translocator domain, membrane protein, outer membrane, beta-domain, beta-barrel
• 由来する生物種: NEISSERIA MENINGITIDIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32460.13

構造登録者

Oomen, C.J.,Van Ulsen, P.,Van Gelder, P.,Feijen, M.,Tommassen, J.,Gros, P. (登録日: 2004-03-02, 公開日: 2004-03-19, 最終更新日: 2024-10-16)

主引用文献

Oomen, C.J.,Van Ulsen, P.,Van Gelder, P.,Feijen, M.,Tommassen, J.,Gros, P.
Structure of the Translocator Domain of a Bacterial Autotransporter
Embo J., 23:1257-, 2004

PubMed Abstract: Autotransporters are virulence-related proteins of Gram-negative bacteria that are secreted via an outer-membrane-based C-terminal extension, the translocator domain. This domain supposedly is sufficient for the transport of the N-terminal passenger domain across the outer membrane. We present here the crystal structure of the in vitro-folded translocator domain of the autotransporter NalP from Neisseria meningitidis, which reveals a 12-stranded beta-barrel with a hydrophilic pore of 10 x 12.5 A that is filled by an N-terminal alpha-helix. The domain has pore activity in vivo and in vitro. Our data are consistent with the model of passenger-domain transport through the hydrophilic channel within the beta-barrel, and inconsistent with a model for transport through a central channel formed by an oligomer of translocator domains. However, the dimensions of the pore imply translocation of the secreted domain in an unfolded form. An alternative model, possibly covering the transport of folded domains, is that passenger-domain transport involves the Omp85 complex, the machinery required for membrane insertion of outer-membrane proteins, on which autotransporters are dependent.

PubMed: 15014442
DOI: 10.1038/SJ.EMBOJ.7600148

実験手法

X-RAY DIFFRACTION (3.2 Å)