Abstract
An interesting recent development is the recognition of a novel ATP-binding superfamily that includes diverse protein families such as DNA topoisomerase II, molecular chaperones Hsp90, DNA-mismatch-repair enzymes MutL and histidine kinases. The most singular unifying feature of this superfamily is the unconventional Bergerat ATP-binding fold. The far-reaching significance of this commonality is still in the process of being explored.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Adenosine Triphosphatases*
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Adenosine Triphosphate / metabolism
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Amino Acid Motifs
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Amino Acid Sequence
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Binding Sites
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Catalytic Domain
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DNA Topoisomerases, Type II / chemistry
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DNA Topoisomerases, Type II / metabolism*
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Escherichia coli Proteins*
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HSP90 Heat-Shock Proteins / chemistry
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HSP90 Heat-Shock Proteins / metabolism*
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Histidine Kinase
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Hydrolysis
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Molecular Sequence Data
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MutL Proteins
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Protein Folding
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Protein Kinases / chemistry
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Protein Kinases / metabolism*
Substances
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Bacterial Proteins
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Escherichia coli Proteins
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HSP90 Heat-Shock Proteins
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MutL protein, E coli
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Adenosine Triphosphate
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Protein Kinases
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Histidine Kinase
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Adenosine Triphosphatases
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MutL Proteins
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DNA Topoisomerases, Type II