1e3m
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(New page: 200px<br /><applet load="1e3m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3m, resolution 2.2Å" /> '''THE CRYSTAL STRUCTURE...)
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Revision as of 11:38, 20 November 2007
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THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A G:T MISMATCH
Overview
DNA mismatch repair ensures genomic integrity on DNA replication., Recognition of a DNA mismatch by a dimeric MutS protein initiates a, cascade of reactions and results in repair of the newly synthesized, strand; however, details of the molecular mechanism remain controversial., Here we present the crystal structure at 2.2 A of MutS from Escherichia, coli bound to a G x T mismatch. The two MutS monomers have different, conformations and form a heterodimer at the structural level. Only one, monomer recognizes the mismatch specifically and has ADP bound. Mismatch, recognition occurs by extensive minor groove interactions causing unusual, base pairing and kinking of the DNA. Nonspecific major groove DNA-binding, domains from both monomers embrace the DNA in a clamp-like structure. The, interleaved nucleotide-binding sites are located far from the DNA., Mutations in human MutS alpha (MSH2/MSH6) that lead to hereditary, predisposition for cancer, such as hereditary non-polyposis colorectal, cancer, can be mapped to this crystal structure.
About this Structure
1E3M is a Single protein structure of sequence from Escherichia coli with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch., Lamers MH, Perrakis A, Enzlin JH, Winterwerp HH, de Wind N, Sixma TK, Nature. 2000 Oct 12;407(6805):711-7. PMID:11048711
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