4CKD
Model of complex between the E.coli enzyme beta-galactosidase and four single chain Fv antibody domains scFv13R4.
Summary for 4CKD
| Entry DOI | 10.2210/pdb4ckd/pdb |
| EMDB information | 2548 |
| Descriptor | BETA-GALACTOSIDASE, SCFV13R4 ANTIBODY FV HEAVY CHAIN, SCFV13R4 ANTIBODY FV LIGHT CHAIN (3 entities in total) |
| Functional Keywords | hydrolase-immune system complex, hydrolase/immune system |
| Biological source | ESCHERICHIA COLI K-12 More |
| Total number of polymer chains | 12 |
| Total formula weight | 564092.87 |
| Authors | Vinothkumar, K.R.,McMullan, G.,Henderson, R. (deposition date: 2014-01-03, release date: 2014-01-15, Last modification date: 2024-10-16) |
| Primary citation | Vinothkumar, K.R.,Mcmullan, G.,Henderson, R. Molecular Mechanism of Antibody-Mediated Activation of Beta-Galactosidase. Structure, 22:621-, 2014 Cited by PubMed Abstract: 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. PubMed: 24613486DOI: 10.1016/J.STR.2014.01.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13 Å) |
Structure validation
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