Crystal structure of a Ca²⁺-dependent regulator of flagellar motility reveals the open-closed structural transition.

ABSTRACT: Sperm chemotaxis toward a chemoattractant is very important for the success of fertilization. Calaxin, a member of the neuronal calcium sensor protein family, directly acts on outer-arm dynein and regulates specific flagellar movement during sperm chemotaxis of ascidian, Ciona intestinalis. Here, we present the crystal structures of calaxin both in the open and closed states upon Ca²⁺ and Mg²⁺ binding. The crystal structures revealed that three of the four EF-hands of a calaxin molecule bound Ca²⁺ ions and that EF2 and EF3 played a critical role in the conformational transition between the open and closed states. The rotation of α7 and α8 helices induces a significant conformational change of a part of the α10 helix into the loop. The structural differences

SUBMITTER: Shojima T 

PROVIDER: S-EPMC5792641 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature