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Binding of Ligand or Monoclonal Antibody 4B1 Induces Discrete Structural Changes in the Lactose Permease of Escherichia coli †

✍ Scribed by Frillingos, Stathis; Wu, Jianhua; Venkatesan, Pushpa; Kaback, H. Ronald

Book ID
127192022
Publisher
American Chemical Society
Year
1997
Tongue
English
Weight
210 KB
Volume
36
Category
Article
ISSN
0006-2960

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The conformationally sensitive epitope for monoclonal antibody (mAb) 4B1, which uncouples lactose from H+ translocation in the lactose permease of Escherichia coli, is localized in the periplasmic loop between helices VII and VIII (loop VII/VIII) on one face of a short helical segment (Sun J, et al.

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## Abstract Lactose transport in membrane vesicles containing lactose permease with a single Cys residue in place of Val 315 is inactivated by __N__‐ethylmaleimide in a manner that is stimulated by substrate or by a H^+^ electrochemical gradient (δμ, Sahin‐Tóth M, Kaback HR, 1993, __Protein Sci 2__

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