Direct interaction of a chaperone-bound type III secretion substrate with the export gate
Recruitment of substrates to virulent bacterial type III secretion systems remains enigmatic. Here, a crystal structure reveals two binding sites between a secretion substrate in complex with its chaperone and the cytosolic domain of the export gate.
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-30487-1 |
| _version_ | 1818235050209050624 |
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| author | Dominic Gilzer Madeleine Schreiner Hartmut H. Niemann |
| author_facet | Dominic Gilzer Madeleine Schreiner Hartmut H. Niemann |
| author_sort | Dominic Gilzer |
| collection | DOAJ |
| description | Recruitment of substrates to virulent bacterial type III secretion systems remains enigmatic. Here, a crystal structure reveals two binding sites between a secretion substrate in complex with its chaperone and the cytosolic domain of the export gate. |
| first_indexed | 2024-12-12T11:47:48Z |
| format | Article |
| id | doaj.art-563d4199679042c89f7bdd65419b5226 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-12T11:47:48Z |
| publishDate | 2022-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-563d4199679042c89f7bdd65419b52262022-12-22T00:25:25ZengNature PortfolioNature Communications2041-17232022-06-0113111310.1038/s41467-022-30487-1Direct interaction of a chaperone-bound type III secretion substrate with the export gateDominic Gilzer0Madeleine Schreiner1Hartmut H. Niemann2Department of Chemistry, Bielefeld UniversityDepartment of Chemistry, Bielefeld UniversityDepartment of Chemistry, Bielefeld UniversityRecruitment of substrates to virulent bacterial type III secretion systems remains enigmatic. Here, a crystal structure reveals two binding sites between a secretion substrate in complex with its chaperone and the cytosolic domain of the export gate.https://doi.org/10.1038/s41467-022-30487-1 |
| spellingShingle | Dominic Gilzer Madeleine Schreiner Hartmut H. Niemann Direct interaction of a chaperone-bound type III secretion substrate with the export gate Nature Communications |
| title | Direct interaction of a chaperone-bound type III secretion substrate with the export gate |
| title_full | Direct interaction of a chaperone-bound type III secretion substrate with the export gate |
| title_fullStr | Direct interaction of a chaperone-bound type III secretion substrate with the export gate |
| title_full_unstemmed | Direct interaction of a chaperone-bound type III secretion substrate with the export gate |
| title_short | Direct interaction of a chaperone-bound type III secretion substrate with the export gate |
| title_sort | direct interaction of a chaperone bound type iii secretion substrate with the export gate |
| url | https://doi.org/10.1038/s41467-022-30487-1 |
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