期刊
SCIENCE
卷 311, 期 5764, 页码 1153-1157出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1120288
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资金
- NCI NIH HHS [R01 CA100742] Funding Source: Medline
- NIGMS NIH HHS [F32 GM067380, R01 GM044853, GM044853] Funding Source: Medline
DNA glycosylases must interrogate millions of base pairs of undamaged DNA in order to locate and then excise one damaged nucleobase. The nature of this search process remains poorly understood. Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial. DNA glycosylase, MutM, interrogating undamaged DNA. These structures, solved to 2.0 angstrom resolution, reveal the nature of the search process: The protein inserts a probe residue into the helical stack and severely buckles the target base pair, which remains intrahelical. MutM therefore actively interrogates the intact DNA helix white searching for damage.
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