Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair.

ABSTRACT: MutL assists the mismatch recognition protein MutS to initiate and coordinate mismatch repair in species ranging from bacteria to humans. The MutL N-terminal ATPase domain is highly conserved, but the C-terminal region shares little sequence similarity among MutL homologs. We report here the crystal structure of the Escherichia coli MutL C-terminal dimerization domain and the likelihood of its conservation among MutL homologs. A 100-residue proline-rich linker between the ATPase and dimerization domains, which generates a large central cavity in MutL dimers, tolerates sequence substitutions and deletions of one-third of its length with no functional consequences in vivo or in vitro. Along the surface of the central cavity, residues essential for DNA binding are located in both the N- and C

SUBMITTER: Guarne A 

PROVIDER: S-EPMC524388 | biostudies-literature | 2004 Oct

REPOSITORIES: biostudies-literature