1Z5C

Topoisomerase VI-B, ADP Pi bound dimer form

Summary for 1Z5C

• Entry DOI: 10.2210/pdb1z5c/pdb
• Related: 1MU5 1MX0 1Z59 1Z5A 1Z5B
• Descriptor: Type II DNA topoisomerase VI subunit B, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: topoisomerase, archaea, atpase, isomerase
• Biological source: Sulfolobus shibatae
• Total number of polymer chains: 2
• Total formula weight: 108582.63

Authors

Corbett, K.D.,Berger, J.M. (deposition date: 2005-03-17, release date: 2005-06-14, Last modification date: 2023-11-15)

Primary citation

Corbett, K.D.,Berger, J.M.
Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI.
Structure, 13:873-882, 2005

PubMed Abstract: GHL proteins are functionally diverse enzymes defined by the presence of a conserved ATPase domain that self-associates to trap substrate upon nucleotide binding. The structural states adopted by these enzymes during nucleotide hydrolysis and product release, and their consequences for enzyme catalysis, have remained unclear. Here, we have determined a complete structural map of the ATP turnover cycle for topoVI-B, the ATPase subunit of the archaeal GHL enzyme topoisomerase VI. With this ensemble of structures, we show that significant conformational changes in the subunit occur first upon ATP binding, and subsequently upon release of hydrolyzed P(i). Together, these data provide a structural framework for understanding the role of ATP hydrolysis in the type II topoisomerase reaction. Our results also suggest that the GHL ATPase module is a molecular switch in which ATP hydrolysis serves as a prerequisite but not a driving force for substrate-dependent structural transitions in the enzyme.

PubMed: 15939019
DOI: 10.1016/j.str.2005.03.013

Experimental method

X-RAY DIFFRACTION (2.2 Å)