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==Overview==

We have refined a series of isomorphous crystal structures of the, Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all, these structures, the DNA is kinked by approximately 60 degrees upon, protein binding. Two residues widely conserved in the MutS family are, involved in mismatch recognition. The phenylalanine, Phe 36, is seen, stacking on one of the mismatched bases. The same base is also seen, forming a hydrogen bond to the glutamate Glu 38. This hydrogen bond, involves the N7 if the base stacking on Phe 36 is a purine and the N3 if, it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to, recognize a wide range of mismatches.

We have refined a series of isomorphous crystal structures of the Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all these structures, the DNA is kinked by approximately 60 degrees upon protein binding. Two residues widely conserved in the MutS family are involved in mismatch recognition. The phenylalanine, Phe 36, is seen stacking on one of the mismatched bases. The same base is also seen forming a hydrogen bond to the glutamate Glu 38. This hydrogen bond involves the N7 if the base stacking on Phe 36 is a purine and the N3 if it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to recognize a wide range of mismatches.

==About this Structure==

Line 14:

[[Category: Protein complex]]

[[Category: Enzlin, J.]]

[[Category: Lamers, M.H.]]

[[Category: Lamers, M H.]]

[[Category: Natrajan, G.]]

[[Category: Perrakis, A.]]

[[Category: Sixma, T.K.]]

[[Category: Sixma, T K.]]

[[Category: Winterwerp, H.H.K.]]

[[Category: Winterwerp, H H.K.]]

[[Category: ADP]]

[[Category: MG]]

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[[Category: mismatch recognition]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:41 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We have refined a series of isomorphous crystal structures of the, Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all, these structures, the DNA is kinked by approximately 60 degrees upon, protein binding. Two residues widely conserved in the MutS family are, involved in mismatch recognition. The phenylalanine, Phe 36, is seen, stacking on one of the mismatched bases. The same base is also seen, forming a hydrogen bond to the glutamate Glu 38. This hydrogen bond, involves the N7 if the base stacking on Phe 36 is a purine and the N3 if, it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to, recognize a wide range of mismatches.
+We have refined a series of isomorphous crystal structures of the Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all these structures, the DNA is kinked by approximately 60 degrees upon protein binding. Two residues widely conserved in the MutS family are involved in mismatch recognition. The phenylalanine, Phe 36, is seen stacking on one of the mismatched bases. The same base is also seen forming a hydrogen bond to the glutamate Glu 38. This hydrogen bond involves the N7 if the base stacking on Phe 36 is a purine and the N3 if it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to recognize a wide range of mismatches.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Enzlin, J.]]
-[[Category: Lamers, M.H.]]
+[[Category: Lamers, M H.]]
 [[Category: Natrajan, G.]]
 [[Category: Perrakis, A.]]
-[[Category: Sixma, T.K.]]
+[[Category: Sixma, T K.]]
-[[Category: Winterwerp, H.H.K.]]
+[[Category: Winterwerp, H H.K.]]
 [[Category: ADP]]
 [[Category: MG]]
@@ Line 24: / Line 24: @@
 [[Category: mismatch recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:58:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:41 2008''