1oh7: Difference between revisions

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~~'''~~THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G MISMATCH~~'''~~

===THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G MISMATCH===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12907723}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12907723 is the PubMed ID number.

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==About this Structure==

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[[Category: Dna binding]]

[[Category: Mismatch recognition]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:50:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:52:53 2008''

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-[[Image:1oh7.jpg|left|200px]]
+{{Seed}}
+[[Image:1oh7.png|left|200px]]
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 {{STRUCTURE_1oh7|  PDB=1oh7  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G MISMATCH'''
+===THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:G MISMATCH===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12907723}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12907723 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12907723}}
 ==About this Structure==
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 [[Category: Dna binding]]
 [[Category: Mismatch recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:50:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:52:53 2008''