1BKN

CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL

Summary for 1BKN

• Entry DOI: 10.2210/pdb1bkn/pdb
• Descriptor: MUTL (2 entities in total)
• Functional Keywords: dna repair, atpase, dna binding
• Biological source: Escherichia coli K12
• Total number of polymer chains: 2
• Total formula weight: 78599.20

Authors

Yang, W.,Ban, C. (deposition date: 1998-07-09, release date: 1999-05-11, Last modification date: 2024-02-07)

Primary citation

Ban, C.,Yang, W.
Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis.
Cell(Cambridge,Mass.), 95:541-552, 1998

PubMed Abstract: MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.

PubMed: 9827806
DOI: 10.1016/S0092-8674(00)81621-9

Experimental method

X-RAY DIFFRACTION (2.9 Å)