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 tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography

C C Hyde1, E W Miles

  • 1Laboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.

Bio/Technology (Nature Publishing Company)
|January 1, 1990
PubMed
Summary

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

Dynamics of laser-induced electroconvection pulses.

Physical review. E, Statistical, nonlinear, and soft matter physics·2004
Same author

Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.

Chemical record (New York, N.Y.)·2002
Same author

Crystallization and preliminary X-ray analysis of human transglutaminase 3 from zymogen to active form.

Journal of structural biology·2001
Same author

The reaction of yeast cystathionine beta-synthase is rate-limited by the conversion of aminoacrylate to cystathionine.

Biochemistry·2001
Same author

Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.

Biochemistry·2001
Same author

Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics.

Biochemistry·2001

Tryptophan synthase alpha 2 beta 2 complex channels indole between active sites. Structural and mutagenesis studies reveal its mechanism and protein interactions for tryptophan biosynthesis.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Tryptophan synthase alpha 2 beta 2 complex catalyzes key steps in tryptophan biosynthesis.
  • This complex exemplifies metabolic intermediate channeling between active sites.

Purpose of the Study:

  • To elucidate the three-dimensional structure of the tryptophan synthase alpha 2 beta 2 complex.
  • To investigate the mechanism of indole channeling and catalysis through structural and mutagenesis approaches.

Main Methods:

  • X-ray crystallography to determine the complex's structure.
  • Site-directed mutagenesis to probe active site residue functions.
  • Recombinant DNA technology for protein interaction and folding studies.

Main Results:

Related Experiment Videos

  • The alpha 2 beta 2 complex has an extended alpha beta beta alpha arrangement (150 A long).
  • Active sites are separated by ~30 A, connected by a potential indole-transfer tunnel.
  • Key residues identified in alpha subunit active sites through genetic studies.

Conclusions:

  • Structural data supports a model for intramolecular indole transfer.
  • Mutagenesis studies are crucial for understanding catalytic mechanisms.
  • Recombinant DNA technology offers further insights into complex assembly and function.