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TitleMolecular mechanism of antibody-mediated activation of β-galactosidase.
Journal, issue, pagesStructure, Vol. 22, Issue 4, Page 621-627, Year 2014
Publish dateApr 8, 2014
AuthorsKutti R Vinothkumar / Greg McMullan / Richard Henderson /
PubMed AbstractBinding of a single-chain Fv antibody to Escherichia coli β-galactosidase (β-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated ...Binding of a single-chain Fv antibody to Escherichia coli β-galactosidase (β-gal) is known to stabilize the enzyme and activate several inactive point mutants, historically called antibody-mediated enzyme formation mutants. To understand the nature of this activation, we have determined by electron cryo-microscopy the structure of the complex between β-gal and the antibody scFv13R4. Our structure localizes the scFv13R4 binding site to the crevice between domains 1 and 3 in each β-gal subunit. The mutations that scFv13R4 counteracts are located between the antibody binding site and the active site of β-gal, at one end of the TIM-barrel that forms domain 3 where the substrate lactose is hydrolyzed. The mode of binding suggests how scFv stabilizes both the active site of β-gal and the tetrameric state.
External linksStructure / PubMed:24613486 / PubMed Central
MethodsEM (single particle)
Resolution13.0 Å
Structure data

2548

4ckd

EMDB-2548: Single particle electron cryomicroscopy of the complex between the E.coli enzyme beta-galactosidase and the single chain Fv antibody scFv13R4.
PDB-4ckd: Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.
Method: EM (single particle) / Resolution: 13.0 Å

Source
  • Escherichia coli (E. coli)
  • mus musculus (house mouse)
  • escherichia coli k-12 (bacteria)
KeywordsHYDROLASE/IMMUNE SYSTEM / HYDROLASE-IMMUNE SYSTEM COMPLEX

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