1SUU

Structure of DNA gyrase A C-terminal domain

Summary for 1SUU

• Entry DOI: 10.2210/pdb1suu/pdb
• Descriptor: DNA gyrase subunit A (2 entities in total)
• Functional Keywords: topoisomerase, dna gyrase, beta-propeller, beta-pinwheel, isomerase
• Biological source: Borrelia burgdorferi (Lyme disease spirochete)
• Cellular location: Cytoplasm (Potential): O51396
• Total number of polymer chains: 1
• Total formula weight: 34508.72

Authors

Corbett, K.D.,Shultzaberger, R.K.,Berger, J.M. (deposition date: 2004-03-26, release date: 2004-04-27, Last modification date: 2024-02-14)

Primary citation

Corbett, K.D.,Shultzaberger, R.K.,Berger, J.M.
The C-terminal domain of DNA gyrase A adopts a DNA-bending beta-pinwheel fold.
Proc.Natl.Acad.Sci.Usa, 101:7293-7298, 2004

PubMed Abstract: DNA gyrase is unique among enzymes for its ability to actively introduce negative supercoils into DNA. This function is mediated in part by the C-terminal domain of its A subunit (GyrA CTD). Here, we report the crystal structure of this approximately 35-kDa domain determined to 1.75-A resolution. The GyrA CTD unexpectedly adopts an unusual fold, which we term a beta-pinwheel, that is globally reminiscent of a beta-propeller but is built of blades with a previously unobserved topology. A large, conserved basic patch on the outer edge of this domain suggests a likely site for binding and bending DNA; fluorescence resonance energy transfer-based assays show that the GyrA CTD is capable of bending DNA by > or =180 degrees over a 40-bp region. Surprisingly, we find that the CTD of the topoisomerase IV A subunit, which shares limited sequence homology with the GyrA CTD, also bends DNA. Together, these data provide a physical explanation for the ability of DNA gyrase to constrain a positive superhelical DNA wrap, and also suggest that the particular substrate preferences of topoisomerase IV might be dictated in part by the function of this domain.

PubMed: 15123801
DOI: 10.1073/pnas.0401595101

Experimental method

X-RAY DIFFRACTION (1.75 Å)