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Conformational dynamics of the essential sensor histidine kinase WalK
Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, w...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5633905/ https://www.ncbi.nlm.nih.gov/pubmed/28994408 http://dx.doi.org/10.1107/S2059798317013043 |
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author | Cai, Yongfei Su, Mingyang Ahmad, Ashfaq Hu, Xiaojie Sang, Jiayan Kong, Lingyuan Chen, Xingqiang Wang, Chen Shuai, Jianwei Han, Aidong |
author_facet | Cai, Yongfei Su, Mingyang Ahmad, Ashfaq Hu, Xiaojie Sang, Jiayan Kong, Lingyuan Chen, Xingqiang Wang, Chen Shuai, Jianwei Han, Aidong |
author_sort | Cai, Yongfei |
collection | PubMed |
description | Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK from Lactobacillus plantarum that shares 60% sequence identity with its homologue VicK from Streptococcus mutans, are presented. WalK adopts an asymmetrical closed structure in the presence of ATP or ADP, in which one of the CA domains is positioned close to the DHp domain, thus leading both the β- and γ-phosphates of ATP/ADP to form hydrogen bonds to the ∊- but not the δ-nitrogen of the phosphorylatable histidine in the DHp domain. In addition, the DHp domain in the ATP/ADP-bound state has a 25.7° asymmetrical helical bending coordinated with the repositioning of the CA domain; these processes are mutually exclusive and alternate in response to helicity changes that are possibly regulated by upstream signals. In the absence of ATP or ADP, however, WalK adopts a completely symmetric open structure with its DHp domain centred between two outward-reaching CA domains. In summary, these structures of WalK reveal the intrinsic dynamic properties of an SK structure as a molecular basis for multifunctionality. |
format | Online Article Text |
id | pubmed-5633905 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-56339052017-10-11 Conformational dynamics of the essential sensor histidine kinase WalK Cai, Yongfei Su, Mingyang Ahmad, Ashfaq Hu, Xiaojie Sang, Jiayan Kong, Lingyuan Chen, Xingqiang Wang, Chen Shuai, Jianwei Han, Aidong Acta Crystallogr D Struct Biol Research Papers Two-component systems (TCSs) are key elements in bacterial signal transduction in response to environmental stresses. TCSs generally consist of sensor histidine kinases (SKs) and their cognate response regulators (RRs). Many SKs exhibit autokinase, phosphoryltransferase and phosphatase activities, which regulate RR activity through a phosphorylation and dephosphorylation cycle. However, how SKs perform different enzymatic activities is poorly understood. Here, several crystal structures of the minimal catalytic region of WalK, an essential SK from Lactobacillus plantarum that shares 60% sequence identity with its homologue VicK from Streptococcus mutans, are presented. WalK adopts an asymmetrical closed structure in the presence of ATP or ADP, in which one of the CA domains is positioned close to the DHp domain, thus leading both the β- and γ-phosphates of ATP/ADP to form hydrogen bonds to the ∊- but not the δ-nitrogen of the phosphorylatable histidine in the DHp domain. In addition, the DHp domain in the ATP/ADP-bound state has a 25.7° asymmetrical helical bending coordinated with the repositioning of the CA domain; these processes are mutually exclusive and alternate in response to helicity changes that are possibly regulated by upstream signals. In the absence of ATP or ADP, however, WalK adopts a completely symmetric open structure with its DHp domain centred between two outward-reaching CA domains. In summary, these structures of WalK reveal the intrinsic dynamic properties of an SK structure as a molecular basis for multifunctionality. International Union of Crystallography 2017-09-27 /pmc/articles/PMC5633905/ /pubmed/28994408 http://dx.doi.org/10.1107/S2059798317013043 Text en © Cai et al. 2017 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Papers Cai, Yongfei Su, Mingyang Ahmad, Ashfaq Hu, Xiaojie Sang, Jiayan Kong, Lingyuan Chen, Xingqiang Wang, Chen Shuai, Jianwei Han, Aidong Conformational dynamics of the essential sensor histidine kinase WalK |
title | Conformational dynamics of the essential sensor histidine kinase WalK |
title_full | Conformational dynamics of the essential sensor histidine kinase WalK |
title_fullStr | Conformational dynamics of the essential sensor histidine kinase WalK |
title_full_unstemmed | Conformational dynamics of the essential sensor histidine kinase WalK |
title_short | Conformational dynamics of the essential sensor histidine kinase WalK |
title_sort | conformational dynamics of the essential sensor histidine kinase walk |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5633905/ https://www.ncbi.nlm.nih.gov/pubmed/28994408 http://dx.doi.org/10.1107/S2059798317013043 |
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