1h7u
From Proteopedia
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'''HPMS2-ATPGS''' | '''HPMS2-ATPGS''' | ||
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[[Category: Junop, M S.]] | [[Category: Junop, M S.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
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Revision as of 15:32, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 18:32:44 2008
