4L9D

Crystal structure of the PKD1 domain from Vibrio cholerae metalloprotease PrtV

4L9D の概要

• エントリーDOI: 10.2210/pdb4l9d/pdb
• 分子名称: Protease, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: pkd domain, cell adhesion
• 由来する生物種: Vibrio cholerae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19205.79

構造登録者

Edwin, A.,Stier, G.,Sauer-Eriksson, A.E. (登録日: 2013-06-18, 公開日: 2013-07-10, 最終更新日: 2024-02-28)

主引用文献

Edwin, A.,Rompikuntal, P.,Bjorn, E.,Stier, G.,Wai, S.N.,Sauer-Eriksson, A.E.
Calcium binding by the PKD1 domain regulates interdomain flexibility in Vibrio cholerae metalloprotease PrtV.
FEBS Open Bio, 3:263-270, 2013

PubMed Abstract: Vibrio cholerae, the causative agent of cholera, releases several virulence factors including secreted proteases when it infects its host. These factors attack host cell proteins and break down tissue barriers and cellular matrix components such as collagen, laminin, fibronectin, keratin, elastin, and they induce necrotic tissue damage. The secreted protease PrtV constitutes one virulence factors of V. cholerae. It is a metalloprotease belonging to the M6 peptidase family. The protein is expressed as an inactive, multidomain, 102 kDa pre-pro-protein that undergoes several N- and C-terminal modifications after which it is secreted as an intermediate variant of 81 kDa. After secretion from the bacteria, additional proteolytic steps occur to produce the 55 kDa active M6 metalloprotease. The domain arrangement of PrtV is likely to play an important role in these maturation steps, which are known to be regulated by calcium. However, the molecular mechanism by which calcium controls proteolysis is unknown. In this study, we report the atomic resolution crystal structure of the PKD1 domain from V. cholera PrtV (residues 755-838) determined at 1.1 Å. The structure reveals a previously uncharacterized Ca(2+)-binding site located near linker regions between domains. Conformational changes in the Ca(2+)-free and Ca(2+)-bound forms suggest that Ca(2+)-binding at the PKD1 domain controls domain linker flexibility, and plays an important structural role, providing stability to the PrtV protein.

PubMed: 23905008
DOI: 10.1016/j.fob.2013.06.003

実験手法

X-RAY DIFFRACTION (1.1 Å)