CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage
Gyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage even...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2018-11-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/41215 |
| _version_ | 1818024087846387712 |
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| author | Katarzyna M Soczek Tim Grant Peter B Rosenthal Alfonso Mondragón |
| author_facet | Katarzyna M Soczek Tim Grant Peter B Rosenthal Alfonso Mondragón |
| author_sort | Katarzyna M Soczek |
| collection | DOAJ |
| description | Gyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage events. Structures where the transported DNA molecule (T-segment) is trapped by the A subunit have not been observed. Here we present the cryoEM structures of two oligomeric complexes of open gyrase A dimers and DNA. The protein subunits in these complexes were solved to 4 Å and 5.2 Å resolution. One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate. The structures locate the T-segment in important intermediate conformations of the catalytic cycle and provide insights into gyrase-DNA interactions and mechanism. |
| first_indexed | 2024-12-10T03:54:39Z |
| format | Article |
| id | doaj.art-8249dafc9a8140d1bbbb7ffd690e5e61 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-12-10T03:54:39Z |
| publishDate | 2018-11-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-8249dafc9a8140d1bbbb7ffd690e5e612022-12-22T02:03:09ZengeLife Sciences Publications LtdeLife2050-084X2018-11-01710.7554/eLife.41215CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passageKatarzyna M Soczek0https://orcid.org/0000-0003-3803-6079Tim Grant1https://orcid.org/0000-0002-4855-8703Peter B Rosenthal2https://orcid.org/0000-0002-0387-2862Alfonso Mondragón3https://orcid.org/0000-0002-0423-6323Department of Molecular Biosciences, Northwestern University, Evanston, United StatesDivision of Physical Biochemistry, MRC National Institute for Medical Research, London, United KingdomDivision of Physical Biochemistry, MRC National Institute for Medical Research, London, United Kingdom; Structural Biology of Cells and Viruses Laboratory, The Francis Crick Institute, London, United KingdomDepartment of Molecular Biosciences, Northwestern University, Evanston, United StatesGyrase is a unique type IIA topoisomerase that uses ATP hydrolysis to maintain the negatively supercoiled state of bacterial DNA. In order to perform its function, gyrase undergoes a sequence of conformational changes that consist of concerted gate openings, DNA cleavage, and DNA strand passage events. Structures where the transported DNA molecule (T-segment) is trapped by the A subunit have not been observed. Here we present the cryoEM structures of two oligomeric complexes of open gyrase A dimers and DNA. The protein subunits in these complexes were solved to 4 Å and 5.2 Å resolution. One of the complexes traps a linear DNA molecule, a putative T-segment, which interacts with the open gyrase A dimers in two states, representing steps either prior to or after passage through the DNA-gate. The structures locate the T-segment in important intermediate conformations of the catalytic cycle and provide insights into gyrase-DNA interactions and mechanism.https://elifesciences.org/articles/41215gyrasetopoisomerasescryoEMB. subtilisstructureT-segment |
| spellingShingle | Katarzyna M Soczek Tim Grant Peter B Rosenthal Alfonso Mondragón CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage eLife gyrase topoisomerases cryoEM B. subtilis structure T-segment |
| title | CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage |
| title_full | CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage |
| title_fullStr | CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage |
| title_full_unstemmed | CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage |
| title_short | CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage |
| title_sort | cryoem structures of open dimers of gyrase a in complex with dna illuminate mechanism of strand passage |
| topic | gyrase topoisomerases cryoEM B. subtilis structure T-segment |
| url | https://elifesciences.org/articles/41215 |
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