1B79
N-TERMINAL DOMAIN OF DNA REPLICATION PROTEIN DNAB
Summary for 1B79
Entry DOI | 10.2210/pdb1b79/pdb |
Descriptor | DnaB Helicase (2 entities in total) |
Functional Keywords | helicase, hexamer, dna replication, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 52890.87 |
Authors | Fass, D.,Bogden, C.E.,Berger, J.M. (deposition date: 1999-01-28, release date: 1999-06-30, Last modification date: 2023-12-27) |
Primary citation | Fass, D.,Bogden, C.E.,Berger, J.M. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure Fold.Des., 7:691-698, 1999 Cited by PubMed Abstract: The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This N-terminal domain is required both for interaction with other proteins in the primosome and for DnaB helicase activity. Knowledge of the structure of this domain may contribute to an understanding of its role in DnaB function. PubMed: 10404598DOI: 10.1016/S0969-2126(99)80090-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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