3ZUA

A C39-like domain

3ZUA の概要

• エントリーDOI: 10.2210/pdb3zua/pdb
• NMR情報: BMRB: 17403
• 分子名称: ALPHA-HEMOLYSIN TRANSLOCATION ATP-BINDING PROTEIN HLYB (1 entity in total)
• 機能のキーワード: c39 peptidase-like domain, abc transporter, haemolysin, hydrolase, heteronuclear nmr
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein (Probable): Q47258
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16106.48

構造登録者

Lecher, J.,Schwarz, C.K.W.,Stoldt, M.,Smits, S.S.H.,Willbold, D.,Schmitt, L. (登録日: 2011-07-18, 公開日: 2012-08-01, 最終更新日: 2024-05-15)

主引用文献

Lecher, J.,Schwarz, C.K.W.,Stoldt, M.,Smits, S.S.H.,Willbold, D.,Schmitt, L.
An Rtx Transporter Tethers its Unfolded Substrate During Secretion Via a Unique N-Terminal Domain.
Structure, 20:1778-, 2012

PubMed Abstract: Type 1 secretion systems (T1SS) catalyze the one step protein transport across the membranes of Gram-negative bacteria and are composed of an outer membrane protein, a membrane fusion protein and an ABC transporter. The ABC transporter consists of the canonical nucleotide binding and transmembrane domains. For the toxin hemolysin A (HlyA), the ABC transporter HlyB carries an additional, N-terminal domain sharing about 40% homology to C39 peptidases, but this "C39-like domain" (CLD) is suggested to feature another, yet unknown function. Our functional and structural analysis demonstrates that the CLD is essential for secretion and that it specifically interacts with the unfolded state of HlyA. We determined the nuclear magnetic resonance structure of the CLD as well as the substrate-binding region within the CLD. This mode of action, represents a mechanism within T1SS and answers the question, how a large and unfolded substrate is protected inside the cells during secretion.

PubMed: 22959622
DOI: 10.1016/J.STR.2012.08.005

実験手法

SOLUTION NMR