1B62

MUTL COMPLEXED WITH ADP

Summary for 1B62

• Entry DOI: 10.2210/pdb1b62/pdb
• Descriptor: PROTEIN (MUTL), MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: dna mismatch repair, atpase
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 40297.71

Authors

Wei, Y. (deposition date: 1999-01-11, release date: 1999-04-28, Last modification date: 2024-04-03)

Primary citation

Ban, C.,Junop, M.,Yang, W.
Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair.
Cell(Cambridge,Mass.), 97:85-97, 1999

PubMed Abstract: 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.

PubMed: 10199405
DOI: 10.1016/S0092-8674(00)80717-5

Experimental method

X-RAY DIFFRACTION (2.1 Å)