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Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition

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...

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Autores principales: Shojima, Tomoki, Hou, Feng, Takahashi, Yusuke, Matsumura, Yoshitaka, Okai, Masahiko, Nakamura, Akira, Mizuno, Katsutoshi, Inaba, Kazuo, Kojima, Masaki, Miyakawa, Takuya, Tanokura, Masaru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5792641/
https://www.ncbi.nlm.nih.gov/pubmed/29386625
http://dx.doi.org/10.1038/s41598-018-19898-7
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author Shojima, Tomoki
Hou, Feng
Takahashi, Yusuke
Matsumura, Yoshitaka
Okai, Masahiko
Nakamura, Akira
Mizuno, Katsutoshi
Inaba, Kazuo
Kojima, Masaki
Miyakawa, Takuya
Tanokura, Masaru
author_facet Shojima, Tomoki
Hou, Feng
Takahashi, Yusuke
Matsumura, Yoshitaka
Okai, Masahiko
Nakamura, Akira
Mizuno, Katsutoshi
Inaba, Kazuo
Kojima, Masaki
Miyakawa, Takuya
Tanokura, Masaru
author_sort Shojima, Tomoki
collection PubMed
description 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 Ca(2+) and Mg(2+) binding. The crystal structures revealed that three of the four EF-hands of a calaxin molecule bound Ca(2+) 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 between the Ca(2+)- and Mg(2+)-bound forms indicates that EF3 in the closed state has a lower affinity for Mg(2+), suggesting that calaxin tends to adopt the open state in Mg(2+)-bound form. SAXS data supports that Ca(2+)-binding causes the structural transition toward the closed state. The changes in the structural transition of the C-terminal domain may be required to bind outer-arm dynein. These results provide a novel mechanism for recognizing a target protein using a calcium sensor protein.
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spelling pubmed-57926412018-02-12 Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition Shojima, Tomoki Hou, Feng Takahashi, Yusuke Matsumura, Yoshitaka Okai, Masahiko Nakamura, Akira Mizuno, Katsutoshi Inaba, Kazuo Kojima, Masaki Miyakawa, Takuya Tanokura, Masaru Sci Rep Article 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 Ca(2+) and Mg(2+) binding. The crystal structures revealed that three of the four EF-hands of a calaxin molecule bound Ca(2+) 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 between the Ca(2+)- and Mg(2+)-bound forms indicates that EF3 in the closed state has a lower affinity for Mg(2+), suggesting that calaxin tends to adopt the open state in Mg(2+)-bound form. SAXS data supports that Ca(2+)-binding causes the structural transition toward the closed state. The changes in the structural transition of the C-terminal domain may be required to bind outer-arm dynein. These results provide a novel mechanism for recognizing a target protein using a calcium sensor protein. Nature Publishing Group UK 2018-01-31 /pmc/articles/PMC5792641/ /pubmed/29386625 http://dx.doi.org/10.1038/s41598-018-19898-7 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Shojima, Tomoki
Hou, Feng
Takahashi, Yusuke
Matsumura, Yoshitaka
Okai, Masahiko
Nakamura, Akira
Mizuno, Katsutoshi
Inaba, Kazuo
Kojima, Masaki
Miyakawa, Takuya
Tanokura, Masaru
Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title_full Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title_fullStr Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title_full_unstemmed Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title_short Crystal structure of a Ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
title_sort crystal structure of a ca(2+)-dependent regulator of flagellar motility reveals the open-closed structural transition
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5792641/
https://www.ncbi.nlm.nih.gov/pubmed/29386625
http://dx.doi.org/10.1038/s41598-018-19898-7
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