Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

What's new with lactose permease

H R Kaback1, K Jung, H Jung

  • 1Howard Hughes Medical Institute, Department of Physiology, University of California Los Angeles 90024-1662.

Journal of Bioenergetics and Biomembranes
|December 1, 1993
PubMed
Summary

Investigating the lactose permease structure in Escherichia coli, this study used site-directed fluorescence labeling. Results reveal close proximity between transmembrane helices, aiding in a new tertiary structure model for this important transport protein.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Measurement of the azimuthal anisotropy of neutral pions in Pb-Pb collisions at sqrt[s](NN)] = 2.76 TeV.

Physical review letters·2014
Same author

Measurement of the Bs(0)→μ+ μ- branching fraction and search for B(0)→μ+ μ- with the CMS experiment.

Physical review letters·2014
Same author

D meson elliptic flow in noncentral Pb-Pb collisions at sqrt[sNN]=2.76 Tev.

Physical review letters·2014
Same author

Search for pair-produced dijet resonances in four-jet final states in pp collisions at sqrt[s] = 7 TeV.

Physical review letters·2014
Same author

Observation of the associated production of a single top quark and a W boson in pp collisions at sqrt[s] = 8 TeV.

Physical review letters·2014
Same author

Novel cosmetic patches for wrinkle improvement: retinyl retinoate- and ascorbic acid-loaded dissolving microneedles.

International journal of cosmetic science·2014

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Dynamics

Background:

  • The lactose permease (LacY) in Escherichia coli is a model for polytopic membrane transporters.
  • Understanding its tertiary structure is crucial for elucidating transport mechanisms.
  • Existing knowledge of LacY's folded structure remains limited.

Purpose of the Study:

  • To investigate the tertiary structure and residue proximity within the lactose permease.
  • To develop a refined structural model of LacY's transmembrane domains.

Main Methods:

  • Site-directed fluorescence labeling using pyrene.
  • Utilizing a cysteine-free mutant of lactose permease.
  • Analyzing pyrene excimer fluorescence to determine residue proximity (<3.5Å).

Related Experiment Videos

Main Results:

  • Demonstrated close proximity between putative helices VIII and IX with helix X.
  • Provided evidence for helix VII being near helices X and XI.
  • These findings support a model for the packing of helices VII to XI.

Conclusions:

  • The tertiary structure model of lactose permease is advanced by proximity data.
  • Specific transmembrane helix interactions are identified.
  • This research contributes to understanding the structural basis of membrane transport.