2f5p: Difference between revisions

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==Overview==

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 while searching, for damage.

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 while searching for damage.

==About this Structure==

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[[Category: Single protein]]

[[Category: Banerjee, A.]]

[[Category: Santos, W.L.]]

[[Category: Santos, W L.]]

[[Category: Verdine, G.L.]]

[[Category: Verdine, G L.]]

[[Category: ZN]]

[[Category: damage search]]

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[[Category: dna repair]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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 while searching, for damage.
+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 while searching for damage.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Banerjee, A.]]
-[[Category: Santos, W.L.]]
+[[Category: Santos, W L.]]
-[[Category: Verdine, G.L.]]
+[[Category: Verdine, G L.]]
 [[Category: ZN]]
 [[Category: damage search]]
@@ Line 23: / Line 23: @@
 [[Category: dna repair]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:28:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:56 2008''