Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2
EF-hand proteins, which contain a Ca2+-binding EF-hand motif, are involved in regulating diverse cellular functions. Ca2+ binding induces conformational changes that modulate the activities of EF-hand proteins. Moreover, these proteins occasionally modify their activities by coordinating metals othe...
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Format: | Article |
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International Union of Crystallography
2023-03-01
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Series: | IUCrJ |
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Online Access: | http://scripts.iucr.org/cgi-bin/paper?S2052252523001501 |
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author | Sang A Mun Jongseo Park Jung Youn Kang Taein Park Minwoo Jin Jihyeong Yang Soo Hyun Eom |
author_facet | Sang A Mun Jongseo Park Jung Youn Kang Taein Park Minwoo Jin Jihyeong Yang Soo Hyun Eom |
author_sort | Sang A Mun |
collection | DOAJ |
description | EF-hand proteins, which contain a Ca2+-binding EF-hand motif, are involved in regulating diverse cellular functions. Ca2+ binding induces conformational changes that modulate the activities of EF-hand proteins. Moreover, these proteins occasionally modify their activities by coordinating metals other than Ca2+, including Mg2+, Pb2+ and Zn2+, within their EF-hands. EFhd1 and EFhd2 are homologous EF-hand proteins with similar structures. Although separately localized within cells, both are actin-binding proteins that modulate F-actin rearrangement through Ca2+-independent actin-binding and Ca2+-dependent actin-bundling activity. Although Ca2+ is known to affect the activities of EFhd1 and EFhd2, it is not known whether their actin-related activities are affected by other metals. Here, the crystal structures of the EFhd1 and EFhd2 core domains coordinating Zn2+ ions within their EF-hands are reported. The presence of Zn2+ within EFhd1 and EFhd2 was confirmed by analyzing anomalous signals and the difference between anomalous signals using data collected at the peak positions as well as low-energy remote positions at the Zn K-edge. EFhd1 and EFhd2 were also found to exhibit Zn2+-independent actin-binding and Zn2+-dependent actin-bundling activity. This suggests the actin-related activities of EFhd1 and EFhd2 could be regulated by Zn2+ as well as Ca2+. |
first_indexed | 2024-04-10T06:10:33Z |
format | Article |
id | doaj.art-52e84f2c3c6b480e8a4912c4adc270e3 |
institution | Directory Open Access Journal |
issn | 2052-2525 |
language | English |
last_indexed | 2024-04-10T06:10:33Z |
publishDate | 2023-03-01 |
publisher | International Union of Crystallography |
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series | IUCrJ |
spelling | doaj.art-52e84f2c3c6b480e8a4912c4adc270e32023-03-02T16:45:22ZengInternational Union of CrystallographyIUCrJ2052-25252023-03-0110223324510.1107/S2052252523001501jt5066Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2Sang A Mun0Jongseo Park1Jung Youn Kang2Taein Park3Minwoo Jin4Jihyeong Yang5Soo Hyun Eom6School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSteitz Center for Structural Biology, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaSchool of Life Sciences, Gwangju Institute of Science and Technology, Gwangju, Republic of KoreaEF-hand proteins, which contain a Ca2+-binding EF-hand motif, are involved in regulating diverse cellular functions. Ca2+ binding induces conformational changes that modulate the activities of EF-hand proteins. Moreover, these proteins occasionally modify their activities by coordinating metals other than Ca2+, including Mg2+, Pb2+ and Zn2+, within their EF-hands. EFhd1 and EFhd2 are homologous EF-hand proteins with similar structures. Although separately localized within cells, both are actin-binding proteins that modulate F-actin rearrangement through Ca2+-independent actin-binding and Ca2+-dependent actin-bundling activity. Although Ca2+ is known to affect the activities of EFhd1 and EFhd2, it is not known whether their actin-related activities are affected by other metals. Here, the crystal structures of the EFhd1 and EFhd2 core domains coordinating Zn2+ ions within their EF-hands are reported. The presence of Zn2+ within EFhd1 and EFhd2 was confirmed by analyzing anomalous signals and the difference between anomalous signals using data collected at the peak positions as well as low-energy remote positions at the Zn K-edge. EFhd1 and EFhd2 were also found to exhibit Zn2+-independent actin-binding and Zn2+-dependent actin-bundling activity. This suggests the actin-related activities of EFhd1 and EFhd2 could be regulated by Zn2+ as well as Ca2+.http://scripts.iucr.org/cgi-bin/paper?S2052252523001501efhd1efhd2crystal structureef-handsactin-binding/bundling protein |
spellingShingle | Sang A Mun Jongseo Park Jung Youn Kang Taein Park Minwoo Jin Jihyeong Yang Soo Hyun Eom Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 IUCrJ efhd1 efhd2 crystal structure ef-hands actin-binding/bundling protein |
title | Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 |
title_full | Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 |
title_fullStr | Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 |
title_full_unstemmed | Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 |
title_short | Structural and biochemical insights into Zn2+-bound EF-hand proteins, EFhd1 and EFhd2 |
title_sort | structural and biochemical insights into zn2 bound ef hand proteins efhd1 and efhd2 |
topic | efhd1 efhd2 crystal structure ef-hands actin-binding/bundling protein |
url | http://scripts.iucr.org/cgi-bin/paper?S2052252523001501 |
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