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

The structural view of bacterial translocation-specific chaperone SecB: implications for function.

Jiahai Zhou1, Zhaohui Xu

  • 1Department of Biological Chemistry, Medical School and Life Sciences Institute, University of Michigan, 210 Washtenaw Avenue, Ann Arbor, MI 48109-2216, USA.

Molecular Microbiology
|October 1, 2005
PubMed
Summary

SecB, a bacterial molecular chaperone, maintains precursor proteins for translocation. Structural studies reveal how SecB binds proteins and interacts with SecA ATPase, explaining its dual role in protein transport.

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

Machine-Learning-Enabled Rapid Evolution of Photoenzymes for the Asymmetric Synthesis of gem-Difluorophosphonates.

Angewandte Chemie (International ed. in English)·2026
Same author

Improved catalytic efficiency of P450 OleP for converting lithocholic acid into murideoxycholic and ursodeoxycholic acids through semi-rational and rational design.

Synthetic and systems biotechnology·2026
Same author

Structure-guided surface engineering to improve the catalytic activity of ethylene-forming enzyme.

Engineering microbiology·2026
Same author

Pea protein isolate as a versatile and sustainable protein: basic characteristics, applications, and limitations.

Food chemistry·2026
Same author

Curdlan, a functionally microbial extracellular polysaccharide with versatile food applications.

Food chemistry·2026
Same author

Asymmetric Reduction of Aryl Ketones by Enzymatic Catalysis with Engineered Ketoreductases.

Organic letters·2026

Area of Science:

  • Bacterial protein translocation
  • Molecular chaperones
  • Structural biology

Background:

  • SecB is a molecular chaperone crucial for bacterial post-translational protein translocation.
  • It ensures precursor polypeptides remain in a translocation-competent state.
  • SecB targets these polypeptides to the translocon by binding both the precursor and the SecA ATPase.

Purpose of the Study:

  • To examine the structural basis of SecB function in protein translocation.
  • To elucidate the molecular interactions between SecB and SecA.
  • To understand the dual role of SecB as a chaperone and targeting factor.

Main Methods:

  • X-ray crystallography to determine SecB and SecB-SecA complex structures.
  • Structural analysis to support existing models of polypeptide binding.

Related Experiment Videos

  • Molecular modeling to propose mechanisms of protein transfer.

    • Main Results:

    • Structures of SecB from H. influenzae and E. coli confirm a two-subsite polypeptide-binding model.
    • A detailed structure of the SecB-SecA complex reveals molecular interactions.
    • A model suggests SecA binding alters SecB conformation, facilitating polypeptide transfer.
    • A second, zinc-independent SecB binding site on SecA was identified.

    Conclusions:

    • Structural insights explain SecB's function as both a chaperone and a targeting factor.
    • The interaction with SecA is key to transferring precursor polypeptides.
    • The newly identified SecA binding site may offer additional functional contributions.