1h7u

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spinqualitylabelsall models 1h7u, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HPMS2-ATPGS

Overview

Human MutLalpha, a heterodimer of hMLH1 and hPMS2, is essential for DNA, mismatch repair. Inactivation of the hmlh1 or hpms2 genes by mutation or, epigenesis causes genomic instability and a predisposition to hereditary, non-polyposis cancer. We report here the X-ray crystal structures of the, conserved N-terminal 40 kDa fragment of hPMS2, NhPMS2, and its complexes, with ATPgammaS and ADP at 1.95, 2.7 and 2.7 A resolution, respectively., The NhPMS2 structures closely resemble the ATPase fragment of Escherichia, coli MutL, which coordinates protein-protein interactions in mismatch, repair by undergoing structural transformation upon binding of ATP. Unlike, the E.coli MutL, whose ATPase activity requires protein dimerization, the, monomeric form of NhPMS2 is active both in ATP hydrolysis and DNA binding., NhPMS2 is the first example of a GHL ATPase active as a monomer, suggesting that its activity may be modulated by hMLH1 in MutLalpha, and, vice versa. The potential heterodimer interface revealed by, crystallography provides a mutagenesis target for functional studies of, MutLalpha.

About this Structure

1H7U is a Single protein structure of sequence from Homo sapiens with MG and ATG as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structure and function of the N-terminal 40 kDa fragment of human PMS2: a monomeric GHL ATPase., Guarne A, Junop MS, Yang W, EMBO J. 2001 Oct 1;20(19):5521-31. PMID:11574484

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