5MDO

Crystal structure of in vitro folded Chitoporin VhChip from Vibrio harveyi (crystal form I)

5MDO の概要

• エントリーDOI: 10.2210/pdb5mdo/pdb
• 分子名称: Chitoporin, SODIUM ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• 機能のキーワード: outer membrane protein, vibrio harveyi, chitin, porin, sugar binding protein
• 由来する生物種: Vibrio harveyi
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 240780.44

構造登録者

Zahn, M.,van den Berg, B. (登録日: 2016-11-13, 公開日: 2017-12-20, 最終更新日: 2024-11-06)

主引用文献

Aunkham, A.,Zahn, M.,Kesireddy, A.,Pothula, K.R.,Schulte, A.,Basle, A.,Kleinekathofer, U.,Suginta, W.,van den Berg, B.
Structural basis for chitin acquisition by marine Vibrio species.
Nat Commun, 9:220-220, 2018

PubMed Abstract: Chitin, an insoluble polymer of N-acetylglucosamine, is one of the most abundant biopolymers on Earth. By degrading chitin, chitinolytic bacteria such as Vibrio harveyi are critical for chitin recycling and maintenance of carbon and nitrogen cycles in the world's oceans. A decisive step in chitin degradation is the uptake of chito-oligosaccharides by an outer membrane protein channel named chitoporin (ChiP). Here, we report X-ray crystal structures of ChiP from V. harveyi in the presence and absence of chito-oligosaccharides. Structures without bound sugar reveal a trimeric assembly with an unprecedented closing of the transport pore by the N-terminus of a neighboring subunit. Substrate binding ejects the pore plug to open the transport channel. Together with molecular dynamics simulations, electrophysiology and in vitro transport assays our data provide an explanation for the exceptional affinity of ChiP for chito-oligosaccharides and point to an important role of the N-terminal gate in substrate transport.

PubMed: 29335469
DOI: 10.1038/s41467-017-02523-y

実験手法

X-RAY DIFFRACTION (1.95 Å)