1bkn
CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTLCRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL
Structural highlights
Function[MUTL_ECOLI] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of the final effector complex. The ATPase activity of MutL is stimulated by DNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMutL 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. Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis.,Ban C, Yang W Cell. 1998 Nov 13;95(4):541-52. PMID:9827806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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