Structural basis of bacterial defense against g-type lysozyme-based innate immunity
Gram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor...
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Birkhäuser Verlag
2013
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Online Access: | https://lirias.kuleuven.be/handle/123456789/362011 https://doi.org/10.1007/s00018-012-1184-1 https://lirias.kuleuven.be/bitstream/123456789/362011/3//leysen_cmls_2012%5B1%5D.pdf |
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ftunivleuven:oai:lirias.kuleuven.be:123456789/362011 2023-05-15T15:32:18+02:00 Structural basis of bacterial defense against g-type lysozyme-based innate immunity Leysen, Seppe Vanderkelen, Lise Weeks, Stephen Michiels, Chris Strelkov, Sergei 2013-03 https://lirias.kuleuven.be/handle/123456789/362011 https://doi.org/10.1007/s00018-012-1184-1 https://lirias.kuleuven.be/bitstream/123456789/362011/3//leysen_cmls_2012%5B1%5D.pdf en eng Birkhäuser Verlag Cellular and Molecular Life Sciences vol:70 issue:6 pages:1113-1122 https://lirias.kuleuven.be/handle/123456789/362011 1420-682X http://dx.doi.org/10.1007/s00018-012-1184-1 1420-9071 https://lirias.kuleuven.be/bitstream/123456789/362011/3//leysen_cmls_2012%5B1%5D.pdf 384762;intranet Article IT 384762;Article 2013 ftunivleuven https://doi.org/10.1007/s00018-012-1184-1 2016-06-13T07:02:43Z Gram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor of g-type lysozyme (PliG-Ec) in complex with Atlantic salmon g-type lysozyme (SalG) at a resolution of 0.95 Å, which is exceptionally high for a complex of two proteins. The structure reveals for the first time the mechanism of g-type lysozyme inhibition by the PliG family. The latter contains two specific conserved regions that are essential for its inhibitory activity. The inhibitory complex formation is based on a double 'key-lock' mechanism. The first key-lock element is formed by the insertion of two conserved PliG regions into the active site of the lysozyme. The second element is defined by a distinct pocket of PliG accommodating a lysozyme loop. Computational analysis indicates that this pocket represents a suitable site for small molecule binding, which opens an avenue for the development of novel antibacterial agents that suppress the inhibitory activity of PliG. status: published Article in Journal/Newspaper Atlantic salmon KU Leuven: Lirias Cellular and Molecular Life Sciences 70 6 1113 1122 |
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Open Polar |
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KU Leuven: Lirias |
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ftunivleuven |
language |
English |
description |
Gram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor of g-type lysozyme (PliG-Ec) in complex with Atlantic salmon g-type lysozyme (SalG) at a resolution of 0.95 Å, which is exceptionally high for a complex of two proteins. The structure reveals for the first time the mechanism of g-type lysozyme inhibition by the PliG family. The latter contains two specific conserved regions that are essential for its inhibitory activity. The inhibitory complex formation is based on a double 'key-lock' mechanism. The first key-lock element is formed by the insertion of two conserved PliG regions into the active site of the lysozyme. The second element is defined by a distinct pocket of PliG accommodating a lysozyme loop. Computational analysis indicates that this pocket represents a suitable site for small molecule binding, which opens an avenue for the development of novel antibacterial agents that suppress the inhibitory activity of PliG. status: published |
format |
Article in Journal/Newspaper |
author |
Leysen, Seppe Vanderkelen, Lise Weeks, Stephen Michiels, Chris Strelkov, Sergei |
spellingShingle |
Leysen, Seppe Vanderkelen, Lise Weeks, Stephen Michiels, Chris Strelkov, Sergei Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
author_facet |
Leysen, Seppe Vanderkelen, Lise Weeks, Stephen Michiels, Chris Strelkov, Sergei |
author_sort |
Leysen, Seppe |
title |
Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
title_short |
Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
title_full |
Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
title_fullStr |
Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
title_full_unstemmed |
Structural basis of bacterial defense against g-type lysozyme-based innate immunity |
title_sort |
structural basis of bacterial defense against g-type lysozyme-based innate immunity |
publisher |
Birkhäuser Verlag |
publishDate |
2013 |
url |
https://lirias.kuleuven.be/handle/123456789/362011 https://doi.org/10.1007/s00018-012-1184-1 https://lirias.kuleuven.be/bitstream/123456789/362011/3//leysen_cmls_2012%5B1%5D.pdf |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_relation |
Cellular and Molecular Life Sciences vol:70 issue:6 pages:1113-1122 https://lirias.kuleuven.be/handle/123456789/362011 1420-682X http://dx.doi.org/10.1007/s00018-012-1184-1 1420-9071 https://lirias.kuleuven.be/bitstream/123456789/362011/3//leysen_cmls_2012%5B1%5D.pdf |
op_rights |
384762;intranet |
op_doi |
https://doi.org/10.1007/s00018-012-1184-1 |
container_title |
Cellular and Molecular Life Sciences |
container_volume |
70 |
container_issue |
6 |
container_start_page |
1113 |
op_container_end_page |
1122 |
_version_ |
1766362810628964352 |