1E3M

The crystal structure of E. coli MutS binding to DNA with a G:T mismatch

Summary for 1E3M

• Entry DOI: 10.2210/pdb1e3m/pdb
• Descriptor: DNA MISMATCH REPAIR PROTEIN MUTS, 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP* GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*AP*T)-3', 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP*GP*AP*CP*AP*CP* TP*GP*GP*TP*GP*CP*TP*TP*GP*GP*CP*AP*GP*CP*T)-3', ... (6 entities in total)
• Functional Keywords: dna binding, mismatch recognition
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 4
• Total formula weight: 200400.40

Authors

Lamers, M.H.,Perrakis, A.,Enzlin, J.H.,Winterwerp, H.H.K.,De Wind, N.,Sixma, T.K. (deposition date: 2000-06-19, release date: 2000-11-01, Last modification date: 2024-10-23)

Primary citation

Lamers, M.H.,Perrakis, A.,Enzlin, J.H.,Winterwerp, H.H.K.,De Wind, N.,Sixma, T.K.
The Crystal Structure of DNA Mismatch Repair Protein Muts Binding to a G X T Mismatch
Nature, 407:711-, 2000

PubMed Abstract: 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.

PubMed: 11048711
DOI: 10.1038/35037523

Experimental method

X-RAY DIFFRACTION (2.2 Å)