Crystal structure of the breakage–reunion domain of dna gyrase

ABSTRACT DNA gyrase is a type II DNA topoisomerase from bacteria that introduces supercoils into DNA1,2. It catalyses the breakage of a DNA duplex (the G segment), the passage of another

segment (the T segment) through the break, and then the reunification of the break. This activity involves the opening and closing of a series of molecular ‘gates’ which is coupled to ATP

hydrolysis. Here we present the crystal structure of the ‘breakage–reunion’ domain of the gyrase at 2.8 Å resolution. Comparison of the structure of this 59K (relative molecular mass,

59,000) domain with that of a 92K fragment of yeast topoisomerase II (ref. 3) reveals a very different quaternary organization, and we propose that the two structures represent two principal

conformations that participate in the enzymatic pathway. The gyrase structure reveals a new dimer contact with a grooved concave surface for binding the G segment and a cluster of conserved

charged residues surrounding the active-site tyrosines. It also shows how breakage of the G segment can occur and, together with the topoisomerase II structure, suggests a pathway by which

the T segment can be released through the second gate of the enzyme. Mutations that confer resistance to the quinolone antibacterial agents cluster at the new dimer interface, indicating how

these drugs might interact with the gyrase–DNA complex. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS

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institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS CRYO-EM STRUCTURES OF THE SPO11 CORE COMPLEX BOUND TO DNA Article Open access 20

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(1992)). Download references ACKNOWLEDGEMENTS We thank C. Petosa, S. Kampranis, L. Bankston and M. Sutcliffe for discussion. We acknowledge the EMBL Hamburg outstation c/o DESY and the SRS

in Daresbury for access to their faciities. This work was supported by the BBSRC. A.M. is a Lister Institute Jenner Fellow. AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Department of

Biochemistry, University of Leicester, LE1 7RH, Leicester, UK Joo H. Morais Cabral, Andrew P. Jackson, Clare V. Smith, Nita Shikotra, Anthony Maxwell & Robert C. Liddington AUTHOR NOTES

* CORRESPONDENCE AND REQUESTS FOR MATERIALS SHOULD BE ADDRESSED TO R.C.L. COORDINATES HAVE BEEN DEPOSITED WITH THE PROTEIN DATABANK (1AB4). Authors * Joo H. Morais Cabral View author

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Smith View author publications You can also search for this author inPubMed Google Scholar * Nita Shikotra View author publications You can also search for this author inPubMed Google

Scholar * Anthony Maxwell View author publications You can also search for this author inPubMed Google Scholar * Robert C. Liddington View author publications You can also search for this

author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Robert C. Liddington. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Cabral, J.,

Jackson, A., Smith, C. _et al._ Crystal structure of the breakage–reunion domain of DNA gyrase. _Nature_ 388, 903–906 (1997). https://doi.org/10.1038/42294 Download citation * Received: 20

February 1997 * Accepted: 05 June 1997 * Issue Date: 28 August 1997 * DOI: https://doi.org/10.1038/42294 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this

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