Relating Structure to Function Through the Dominant Slow Modes of Motion of DNA Topoisomerase II

R. L. Jernigan, Melik C. Demirel, I. Bahar

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Type II DNA topoisomerases are enzymes capable of transporting one DNA duplex through another by performing a cycle of DNA cleavage, transport, and religation, coupled to ATP binding and hydrolysis. Here, we considered a coarse-grained model of the structure and investigated the motions within two structures, DNA topoisomerase II and DNA gyrase A. The coarse graining with only one point per residue means that motions in such large proteins can be thoroughly investigated. The overall motions are reflected in the crystallographic temperature factors, which are reproduced by the model. Also, with this approach, we can view the slowest, most cooperative, modes of motion, corresponding to the largest-scale correlated motions in the protein. These motions are nearly identical in the two proteins and are likely related to individual steps in the enzyme's complex mechanism of activity.

Original languageEnglish (US)
Pages (from-to)301-312
Number of pages12
JournalInternational Journal of Quantum Chemistry
Volume75
Issue number3
DOIs
StatePublished - Jan 1 1999

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Type II DNA Topoisomerase
deoxyribonucleic acid
DNA Gyrase
Proteins
DNA
Enzymes
proteins
enzymes
Hydrolysis
Adenosine Triphosphate
adenosine triphosphate
hydrolysis
cleavage
Temperature
cycles

All Science Journal Classification (ASJC) codes

  • Atomic and Molecular Physics, and Optics
  • Condensed Matter Physics
  • Physical and Theoretical Chemistry

Cite this

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Relating Structure to Function Through the Dominant Slow Modes of Motion of DNA Topoisomerase II. / Jernigan, R. L.; Demirel, Melik C.; Bahar, I.

In: International Journal of Quantum Chemistry, Vol. 75, No. 3, 01.01.1999, p. 301-312.

Research output: Contribution to journalArticle

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