4ZM8

Crystal Structure of Sialostatin L

「3LI7」から置き換えられました

4ZM8 の概要

• エントリーDOI: 10.2210/pdb4zm8/pdb
• 分子名称: Putative secreted cystatin (2 entities in total)
• 機能のキーワード: cystatin, tick, protease inhibitor, hydrolase inhibitor
• 由来する生物種: Ixodes scapularis (Black-legged tick)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49662.68

構造登録者

Andersen, J.F.,Kosyfakis, M. (登録日: 2015-05-02, 公開日: 2015-06-17, 最終更新日: 2024-10-30)

主引用文献

Kotsyfakis, M.,Horka, H.,Salat, J.,Andersen, J.F.
The crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model.
Mol. Microbiol., 77:456-470, 2010

PubMed Abstract: We have previously demonstrated that two salivary cysteine protease inhibitors from the Borrelia burgdorferi (Lyme disease) vector Ixodes scapularis- namely sialostatins L and L2 - play an important role in tick biology, as demonstrated by the fact that silencing of both sialostatins in tandem results in severe feeding defects. Here we show that sialostatin L2 - but not sialostatin L - facilitates the growth of B. burgdorferi in murine skin. To examine the structural basis underlying these differential effects of the two sialostatins, we have determined the crystal structures of both sialostatin L and L2. This is the first structural analysis of cystatins from an invertebrate source. Sialostatin L2 crystallizes as a monomer with an 'unusual' conformation of the N-terminus, while sialostatin L crystallizes as a domain-swapped dimer with an N-terminal conformation similar to other cystatins. Deletion of the 'unusual' N-terminal five residues of sialostatin L2 results in marked changes in its selectivity, suggesting that this region is a particularly important determinant of the biochemical activity of sialostatin L2. Collectively, our results reveal the structure of two tick salivary components that facilitate vector blood feeding and that one of them also supports pathogen transmission to the vertebrate host.

PubMed: 20545851
DOI: 10.1111/j.1365-2958.2010.07220.x

実験手法

X-RAY DIFFRACTION (2.6762 Å)