期刊
STRUCTURE
卷 9, 期 1, 页码 47-55出版社
CELL PRESS
DOI: 10.1016/S0969-2126(00)00552-9
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资金
- NIGMS NIH HHS [GM44772] Funding Source: Medline
Background: ATP-mediated cooperative assembly of a RecA nucleoprotein filament activates the protein for catalysis of DNA strand exchange. RecA is a classic allosterically regulated enzyme in that ATP binding results in a dramatic increase in ssDNA binding affinity. This increase in ssDNA binding affinity results almost exclusively from an ATP-mediated increase in cooperative filament assembly rather than an increase in the inherent affinity of monomeric RecA for DNA. Therefore, certain residues at the subunit interface must play an important role in transmitting allosteric information across the filament structure of RecA.
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