CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage

Katarzyna M. Soczek, Tim Grant, Peter B. Rosenthal, Alfonso Mondragón*

*Corresponding author for this work

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Article numbere41215
JournaleLife
Volume7
DOIs
StatePublished - Nov 1 2018

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Dimers
DNA
DNA Gyrase
Bacterial DNA
DNA Cleavage
Protein Subunits
Molecules
Hydrolysis
Adenosine Triphosphate
Conformations

ASJC Scopus subject areas

  • Neuroscience(all)
  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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title = "CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage",
abstract = "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 {\AA} and 5.2 {\AA} 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.",
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CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage. / Soczek, Katarzyna M.; Grant, Tim; Rosenthal, Peter B.; Mondragón, Alfonso.

In: eLife, Vol. 7, e41215, 01.11.2018.

Research output: Contribution to journalArticle

TY - JOUR

T1 - CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage

AU - Soczek, Katarzyna M.

AU - Grant, Tim

AU - Rosenthal, Peter B.

AU - Mondragón, Alfonso

PY - 2018/11/1

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AB - 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.

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