The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.

Case BC, Hartley S, Osuga M, Jeruzalmi D, Hingorani MM. The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair. Nucleic Acids Res. 2019 05 07; 47(8):4136-4152.

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subject areas

Adenosine Triphosphate
Amino Acid Sequence
Bacterial Proteins
Binding Sites
Cloning, Molecular
DNA Damage
DNA Repair
DNA, Bacterial
Endodeoxyribonucleases
Escherichia coli
Escherichia coli Proteins
Gene Expression
Genetic Vectors
Geobacillus stearothermophilus
Kinetics
Models, Molecular
Protein Binding
Protein Interaction Domains and Motifs
Protein Multimerization
Protein Structure, Secondary
Recombinant Proteins
Sequence Alignment
Structural Homology, Protein
Substrate Specificity
Thermodynamics
Thermotoga maritima

authors with profiles

David Jeruzalmi

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