1oh8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 26: | Line 26: | ||
[[Category: mismatch recognition]] | [[Category: mismatch recognition]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:54:39 2007'' | ||
Revision as of 17:49, 5 November 2007
|
THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH AN UNPAIRED THYMIDINE
OverviewOverview
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 StructureAbout this Structure
1OH8 is a Protein complex structure of sequences from Escherichia coli with MG and ADP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Nov 5 16:54:39 2007