1x9z

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spinqualitylabelsall models 1x9z, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the MutL C-terminal domain

Overview

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-terminal domains. Each domain of MutL, interacts with UvrD helicase and is required for activating the helicase, activity. The DNA-binding capacity of MutL is correlated with the level of, UvrD activation. A model of how MutL utilizes its ATPase and DNA-binding, activities to mediate mismatch-dependent activation of MutH endonuclease, and UvrD helicase is proposed.

About this Structure

1X9Z is a Single protein structure of sequence from Escherichia coli with CL, NA, GOL and IPA as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair., Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W, EMBO J. 2004 Oct 27;23(21):4134-45. Epub 2004 Oct 7. PMID:15470502

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