Mutational Analysis of Mycobacterium UvrD1 Identifies Functional Groups Required for ATP Hydrolysis, DNA Unwinding, and Chemomechanical Coupling
Author:
Affiliation:
1. Molecular Biology Program, Sloan-Kettering Institute
2. Immunology Program, Sloan-Kettering Institute
3. Division of Infectious Diseases, Memorial-Sloan Kettering Cancer Center, New York, New York 10021
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi900103d
Reference32 articles.
1. Structure and Mechanism of Helicases and Nucleic Acid Translocases
2. Major Domain Swiveling Revealed by the Crystal Structures of Complexes of E. coli Rep Helicase Bound to Single-Stranded DNA and ADP
3. Crystal Structures of Complexes of PcrA DNA Helicase with a DNA Substrate Indicate an Inchworm Mechanism
4. UvrD Helicase Unwinds DNA One Base Pair at a Time by a Two-Part Power Stroke
5. Demonstration of Unidirectional Single-Stranded DNA Translocation by PcrA Helicase: Measurement of Step Size and Translocation Speed
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