1b63
From Proteopedia
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MUTL COMPLEXED WITH ADPNP
Overview
The MutL DNA mismatch repair protein has recently been shown to be an, ATPase and to belong to an emerging ATPase superfamily that includes DNA, topoisomerase II and Hsp90. We report here the crystal structures of a 40, kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate, analog, ADPnP, and with product ADP. More than 60 residues that are, disordered in the apoprotein structure become ordered and contribute to, both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified, by subsequent release of the gamma-phosphate, releases two key loops and, leads to dissociation of the LN40 dimer. Dimerization of the LN40 region, is required for and is the rate-limiting step in ATP hydrolysis by MutL., The ATPase activity of MutL is stimulated by DNA and likely acts as a, switch to coordinate DNA mismatch repair.
About this Structure
1B63 is a Single protein structure of sequence from Escherichia coli with MG, EDO and ANP as ligands. Full crystallographic information is available from OCA.
Reference
Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair., Ban C, Junop M, Yang W, Cell. 1999 Apr 2;97(1):85-97. PMID:10199405
Page seeded by OCA on Tue Nov 20 11:23:32 2007
Categories: Escherichia coli | Single protein | Yang, W. | ANP | EDO | MG | Atpase | Dna mismatch repair
