Abstract：
:Ligand-induced allosteric changes in proteins are important in their cellular functions and regulation, and both concerted and sequential examples are known. The distinction has entailed elaborate analysis, however, and only a few systems have been unequivocally analysed. We have investigated the coupling between ATP usage and DNA transport by type II DNA topoisomerases, and one key question concerning allostery in these dyadic enzymes is whether ATP binding to one protomer can induce a concerted conformational change in the entire enzyme. Here we use an enzyme with one immunotagged subunit defective in ATP binding and one wild-type subunit to show that it can. Our approach should be generally applicable in the study of allostery and communication between members of a macromolecular assembly.
journal_name
Naturejournal_title
Natureauthors
Lindsley JE,Wang JCdoi
10.1038/361749a0subject
Has Abstractpub_date
1993-02-25 00:00:00pages
749-50issue
6414eissn
0028-0836issn
1476-4687journal_volume
361pub_type
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