To cleave or not to cleave? Insights from the LexA crystal structure.
In the September 7, 2001 issue of Cell, Luo et al. describe the structure of LexA protein in two states, cleavable and noncleavable. This structure offers new insights into how LexA and other structurally related proteins, such as lambda and UmuD, undergo autocatalytic cleavage using a Ser-Lys dyad.
Walker
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Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge 02139, MA, USA.
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D004247:DNA / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase; D019281:Dimerization; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D006860:Hydrogen Bonding; D009154:Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011938:Rec A Recombinases / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D004247:DNA; D004259:DNA-Directed DNA Polymerase; D029968:Escherichia coli Proteins; D011938:Rec A Recombinases; D012097:Repressor Proteins; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein; C055218:UmuD protein, E coli