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New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex
The complex of two membrane proteins, sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII), mediates negative phototaxis in halobacteria N. pharaonis. Upon light activation NpSRII triggers a signal transduction chain homologous to the two-component system in eubacterial chemotaxis. He...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5292967/ https://www.ncbi.nlm.nih.gov/pubmed/28165484 http://dx.doi.org/10.1038/srep41811 |
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author | Ishchenko, A. Round, E. Borshchevskiy, V. Grudinin, S. Gushchin, I. Klare, J. P. Remeeva, A. Polovinkin, V. Utrobin, P. Balandin, T. Engelhard, M. Büldt, G. Gordeliy, V. |
author_facet | Ishchenko, A. Round, E. Borshchevskiy, V. Grudinin, S. Gushchin, I. Klare, J. P. Remeeva, A. Polovinkin, V. Utrobin, P. Balandin, T. Engelhard, M. Büldt, G. Gordeliy, V. |
author_sort | Ishchenko, A. |
collection | PubMed |
description | The complex of two membrane proteins, sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII), mediates negative phototaxis in halobacteria N. pharaonis. Upon light activation NpSRII triggers a signal transduction chain homologous to the two-component system in eubacterial chemotaxis. Here we report on crystal structures of the ground and active M-state of the complex in the space group I2(1)2(1)2(1). We demonstrate that the relative orientation of symmetrical parts of the dimer is parallel (“U”-shaped) contrary to the gusset-like (“V”-shaped) form of the previously reported structures of the NpSRII/NpHtrII complex in the space group P2(1)2(1)2, although the structures of the monomers taken individually are nearly the same. Computer modeling of the HAMP domain in the obtained “V”- and “U”-shaped structures revealed that only the “U”-shaped conformation allows for tight interactions of the receptor with the HAMP domain. This is in line with existing data and supports biological relevance of the “U” shape in the ground state. We suggest that the “V”-shaped structure may correspond to the active state of the complex and transition from the “U” to the “V”-shape of the receptor-transducer complex can be involved in signal transduction from the receptor to the signaling domain of NpHtrII. |
format | Online Article Text |
id | pubmed-5292967 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-52929672017-02-10 New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex Ishchenko, A. Round, E. Borshchevskiy, V. Grudinin, S. Gushchin, I. Klare, J. P. Remeeva, A. Polovinkin, V. Utrobin, P. Balandin, T. Engelhard, M. Büldt, G. Gordeliy, V. Sci Rep Article The complex of two membrane proteins, sensory rhodopsin II (NpSRII) with its cognate transducer (NpHtrII), mediates negative phototaxis in halobacteria N. pharaonis. Upon light activation NpSRII triggers a signal transduction chain homologous to the two-component system in eubacterial chemotaxis. Here we report on crystal structures of the ground and active M-state of the complex in the space group I2(1)2(1)2(1). We demonstrate that the relative orientation of symmetrical parts of the dimer is parallel (“U”-shaped) contrary to the gusset-like (“V”-shaped) form of the previously reported structures of the NpSRII/NpHtrII complex in the space group P2(1)2(1)2, although the structures of the monomers taken individually are nearly the same. Computer modeling of the HAMP domain in the obtained “V”- and “U”-shaped structures revealed that only the “U”-shaped conformation allows for tight interactions of the receptor with the HAMP domain. This is in line with existing data and supports biological relevance of the “U” shape in the ground state. We suggest that the “V”-shaped structure may correspond to the active state of the complex and transition from the “U” to the “V”-shape of the receptor-transducer complex can be involved in signal transduction from the receptor to the signaling domain of NpHtrII. Nature Publishing Group 2017-02-06 /pmc/articles/PMC5292967/ /pubmed/28165484 http://dx.doi.org/10.1038/srep41811 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Ishchenko, A. Round, E. Borshchevskiy, V. Grudinin, S. Gushchin, I. Klare, J. P. Remeeva, A. Polovinkin, V. Utrobin, P. Balandin, T. Engelhard, M. Büldt, G. Gordeliy, V. New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title | New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title_full | New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title_fullStr | New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title_full_unstemmed | New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title_short | New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex |
title_sort | new insights on signal propagation by sensory rhodopsin ii/transducer complex |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5292967/ https://www.ncbi.nlm.nih.gov/pubmed/28165484 http://dx.doi.org/10.1038/srep41811 |
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