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1B79

N-TERMINAL DOMAIN OF DNA REPLICATION PROTEIN DNAB

Summary for 1B79
Entry DOI10.2210/pdb1b79/pdb
DescriptorDnaB Helicase (2 entities in total)
Functional Keywordshelicase, hexamer, dna replication, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight52890.87
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 citationFass, 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: 10404598
DOI: 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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数据于2025-06-18公开中

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