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

Conserved structural features and sequence patterns in the GroES fold family.

B Taneja1, S C Mande

  • 1Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India.

Protein Engineering
|November 11, 1999
PubMed
Summary

The GroES fold, a protein family including chaperonin-10 and dehydrogenases, maintains its structure via a conserved core and specific residues. Mutations like Ile to Leu within this core are surprisingly non-conservative.

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

Multi-omics analysis identifies potential microbial and metabolite diagnostic biomarkers of bacterial vaginosis.

Journal of the European Academy of Dermatology and Venereology : JEADV·2024
Same author

Discovery of serum biomarkers for diagnosis of tuberculosis by NMR metabolomics including cross-validation with a second cohort.

Biomedical journal·2021
Same author

Terbinafine resistance in dermatophytes: Time to revisit alternate antifungal therapy.

Journal de mycologie medicale·2020
Same author

Active and prospective latent tuberculosis are associated with different metabolomic profiles: clinical potential for the identification of rapid and non-invasive biomarkers.

Emerging microbes & infections·2020
Same author

Non-cardiac surgery 2 weeks after percutaneous cardiac intervention.

British journal of anaesthesia·2009
Same author

The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology.

Tuberculosis (Edinburgh, Scotland)·2003

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • The GroES fold encompasses diverse protein families like chaperonin-10, quinone oxidoreductase, glucose dehydrogenase, and alcohol dehydrogenase.
  • Previous classification identified these proteins as belonging to the GroES fold based on structural similarities.

Purpose of the Study:

  • To conduct an extensive analysis of the sequences and three-dimensional structures of proteins within the GroES fold family.
  • To identify conserved structural elements and key residues critical for maintaining the GroES fold.

Main Methods:

  • Superposition of individual protein structures to assess structural equivalence.
  • Analysis of sequence and structural data to identify conserved hydrophobic cores and key residues.
  • Investigation of mutation patterns, specifically Ile to Leu and Ile to Val, within the protein core.

Related Experiment Videos

Main Results:

  • High structural superposition accuracy (within 1.6 Å for >60 residues) confirms a conserved hydrophobic core.
  • Identification of conserved key residues essential for maintaining the GroES fold.
  • Discovery that Ile to Leu mutations in the protein core are non-conservative, while Ile to Val mutations occur frequently.

Conclusions:

  • A glycyl-aspartate dipeptide is proposed as critical for sustaining the GroES fold.
  • The study highlights the non-conservative nature of specific mutations within the protein core, offering insights into protein stability and evolution.