1oh5
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | We have refined a series of isomorphous crystal structures of the | + | 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== | ==About this Structure== | ||
| Line 14: | Line 14: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Enzlin, J.]] | [[Category: Enzlin, J.]] | ||
| - | [[Category: Lamers, M | + | [[Category: Lamers, M H.]] |
[[Category: Natrajan, G.]] | [[Category: Natrajan, G.]] | ||
[[Category: Perrakis, A.]] | [[Category: Perrakis, A.]] | ||
| - | [[Category: Sixma, T | + | [[Category: Sixma, T K.]] |
| - | [[Category: Winterwerp, H | + | [[Category: Winterwerp, H H.K.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| Line 24: | Line 24: | ||
[[Category: mismatch recognition]] | [[Category: mismatch recognition]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:41 2008'' |
Revision as of 12:17, 21 February 2008
|
THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A 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.
About this Structure
1OH5 is a Protein complex structure of sequences from Escherichia coli with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates., Natrajan G, Lamers MH, Enzlin JH, Winterwerp HH, Perrakis A, Sixma TK, Nucleic Acids Res. 2003 Aug 15;31(16):4814-21. PMID:12907723
Page seeded by OCA on Thu Feb 21 14:17:41 2008
