2fco: Difference between revisions

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==Overview==

Here we report a high resolution structure of RecU-Holliday junction, resolvase from Bacillus stearothermophilus. The functional unit of RecU is, a homodimer that contains a "mushroom" like structure with a rigid cap and, two highly flexible loops extending outwards. These loops appear to be, highly flexible/dynamic, and presumably are directly involved in DNA, binding and holding it for catalysis. Structural modifications of both the, protein and DNA upon their interaction are essential for catalysis. An, Mg2+ ion is present in each of the two active sites in this homodimeric, enzyme, and two water molecules are coordinated with each Mg2+ ion. Our, data are consistent with one of these water molecules acting as a, nucleophile and the other as a general acid. The identities of the general, base and general acid involved in catalysis and the Lewis acid that, stabilizes the pentacovalent transition state phosphate ion are proposed., A model for the RecU-Holliday junction DNA complex is also proposed and, discussed in the context of DNA binding and cleavage.

Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a "mushroom" like structure with a rigid cap and two highly flexible loops extending outwards. These loops appear to be highly flexible/dynamic, and presumably are directly involved in DNA binding and holding it for catalysis. Structural modifications of both the protein and DNA upon their interaction are essential for catalysis. An Mg2+ ion is present in each of the two active sites in this homodimeric enzyme, and two water molecules are coordinated with each Mg2+ ion. Our data are consistent with one of these water molecules acting as a nucleophile and the other as a general acid. The identities of the general base and general acid involved in catalysis and the Lewis acid that stabilizes the pentacovalent transition state phosphate ion are proposed. A model for the RecU-Holliday junction DNA complex is also proposed and discussed in the context of DNA binding and cleavage.

==About this Structure==

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[[Category: Geobacillus kaustophilus]]

[[Category: Single protein]]

[[Category: Jedrzejas, M.J.]]

[[Category: Jedrzejas, M J.]]

[[Category: Li, J.]]

[[Category: EDO]]

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[[Category: hydrolase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Here we report a high resolution structure of RecU-Holliday junction, resolvase from Bacillus stearothermophilus. The functional unit of RecU is, a homodimer that contains a "mushroom" like structure with a rigid cap and, two highly flexible loops extending outwards. These loops appear to be, highly flexible/dynamic, and presumably are directly involved in DNA, binding and holding it for catalysis. Structural modifications of both the, protein and DNA upon their interaction are essential for catalysis. An, Mg2+ ion is present in each of the two active sites in this homodimeric, enzyme, and two water molecules are coordinated with each Mg2+ ion. Our, data are consistent with one of these water molecules acting as a, nucleophile and the other as a general acid. The identities of the general, base and general acid involved in catalysis and the Lewis acid that, stabilizes the pentacovalent transition state phosphate ion are proposed., A model for the RecU-Holliday junction DNA complex is also proposed and, discussed in the context of DNA binding and cleavage.
+Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a "mushroom" like structure with a rigid cap and two highly flexible loops extending outwards. These loops appear to be highly flexible/dynamic, and presumably are directly involved in DNA binding and holding it for catalysis. Structural modifications of both the protein and DNA upon their interaction are essential for catalysis. An Mg2+ ion is present in each of the two active sites in this homodimeric enzyme, and two water molecules are coordinated with each Mg2+ ion. Our data are consistent with one of these water molecules acting as a nucleophile and the other as a general acid. The identities of the general base and general acid involved in catalysis and the Lewis acid that stabilizes the pentacovalent transition state phosphate ion are proposed. A model for the RecU-Holliday junction DNA complex is also proposed and discussed in the context of DNA binding and cleavage.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Geobacillus kaustophilus]]
 [[Category: Single protein]]
-[[Category: Jedrzejas, M.J.]]
+[[Category: Jedrzejas, M J.]]
 [[Category: Li, J.]]
 [[Category: EDO]]
@@ Line 22: / Line 22: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:02:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:02 2008''