Abstract
The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / metabolism
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Crystallography, X-Ray
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DNA / metabolism
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DNA Gyrase
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DNA Topoisomerases, Type II / chemistry*
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DNA Topoisomerases, Type II / metabolism
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Escherichia coli / enzymology
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Protein Binding
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Protein Conformation
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Saccharomyces cerevisiae / enzymology
Substances
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Peptide Fragments
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Adenosine Triphosphate
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DNA
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Adenosine Triphosphatases
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DNA Gyrase
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DNA Topoisomerases, Type II