Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein. Molecular topography of the enzyme.-Reference-Cited by-同舟云学术

Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein. Molecular topography of the enzyme.

Published:1994-12 Issue:50 Volume:269 Page:31359-31371
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bujalowski W,Klonowska M M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

1. Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli.

2. Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA.

3. Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication.

4. Mechanism of dnaB protein action. IV. General priming of DNA replication by dnaB protein and primase compared with RNA polymerase.

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