PMID:11029656
| Citation |
Yoshikawa, M, Iwasaki, H, Kinoshita, K and Shinagawa, H (2000) Two basic residues, Lys-107 and Lys-118, of RuvC resolvase are involved in critical contacts with the Holliday junction for its resolution. Genes Cells 5:803-13 |
|---|---|
| Abstract |
Crystallographic and mutational studies of Escherichia coli RuvC Holliday junction resolvase have revealed that a catalytic site of each subunit is composed of four acidic residues at the bottom of the putative DNA-binding cleft, whose surface contains eight basic residues. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Catalytic Domain; DNA Repair; DNA, Bacterial/metabolism; Endodeoxyribonucleases/chemistry; Endodeoxyribonucleases/genetics; Endodeoxyribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Lysine/chemistry; Magnesium/pharmacology; Manganese/pharmacology; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Sequence Alignment; Sodium Chloride/pharmacology; Temperature |
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