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

Studying enzyme-beta-lactam interactions using X-ray diffraction.

J A Kelly1, J R Knox, H Zhao

  • 1University of Connecticut, Department of Molecular and Cell Biology, Storrs.

Journal of Molecular Graphics
|June 1, 1989
PubMed
Summary
This summary is machine-generated.

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

[Detection of anti-HAV, anti-HBV, anti-HCV and anti-HEV antibodies in the patients with sporadic acute hepatitis in Beijing during 1995-2000].

Zhonghua shi yan he lin chuang bing du xue za zhi = Zhonghua shiyan he linchuang bingduxue zazhi = Chinese journal of experimental and clinical virology·2002
Same author

Chiral synthesis and enzymatic resolution of (S)-(-)piperazine-2-carboxylic acid using enzyme alcalase.

Enantiomer·2002
Same author

[The model of piggyback orthotopic liver transplantation in pigs].

Hunan yi ke da xue xue bao = Hunan yike daxue xuebao = Bulletin of Hunan Medical University·2002
Same author

[The manifestations of 496 cases with thyroid-related immune orbitopathy and normal thyroid function].

[Zhonghua yan ke za zhi] Chinese journal of ophthalmology·2002
Same author

[A study of cytokines in pathogenesis of thyroid-related immune orbitopathy].

[Zhonghua yan ke za zhi] Chinese journal of ophthalmology·2002
Same author

[Analysis of hepatitis G virus genotypes in some areas of China].

Zhonghua yu fang yi xue za zhi [Chinese journal of preventive medicine]·2002
Same journal

HOLE: a program for the analysis of the pore dimensions of ion channel structural models.

Journal of molecular graphics·1996
Same journal

Analytically defined surfaces to analyze molecular interaction properties.

Journal of molecular graphics·1996
Same journal

Prediction of high-frequency electron paramagnetic resonance spectra of spin S = 3/2, 5/2 systems.

Journal of molecular graphics·1996
Same journal

Affecting the activity of soybean lipoxygenase-1.

Journal of molecular graphics·1996
Same journal

Why spin = 1, 2 species have no electron paramagnetic resonance signal under normal conditions: possible detection by electron paramagnetic resonance at frequency close to D value?

Journal of molecular graphics·1996
Same journal

Knowledge-based modeling of a legume lectin and docking of the carbohydrate ligand: the Ulex europaeus lectin I and its interaction with fucose.

Journal of molecular graphics·1996
See all related articles

This study used X-ray diffraction to visualize how beta-lactam antibiotics interact with bacterial enzymes. The findings reveal the enzyme

Area of Science:

  • Biochemistry
  • Structural Biology
  • Medicinal Chemistry

Background:

  • Beta-lactam antibiotics are crucial for treating bacterial infections.
  • Understanding their mechanism of action at a molecular level is vital for developing new drugs.
  • Bacterial resistance necessitates continuous research into antibiotic-enzyme interactions.

Purpose of the Study:

  • To elucidate the three-dimensional structural interactions between beta-lactam antibiotics and a bacterial enzyme target.
  • To investigate the acylation mechanism of the D-alanyl-D-alanine transpeptidase-carboxypeptidase enzyme by different beta-lactam inhibitors.
  • To correlate the stability of antibiotic-enzyme complexes with specific molecular distances.

Main Methods:

  • X-ray diffraction analysis was employed to determine the structures.

Related Experiment Videos

  • Complexes of cephalosporin C, benzylmonobactam, and alpha-(2,3)-methylenepenicillin G with Streptomyces R61 DD-peptidase were analyzed.
  • High-resolution structural data (2.25 A) was obtained.

    • Main Results:

    • The reactive serine residue of the enzyme was found to acylate the beta-lactam ring of each antibiotic inhibitor.
    • Three-dimensional structures revealed the precise binding modes of the antibiotics.
    • A correlation was established between the half-lives of the acyl complexes and the proximity of the antibiotic's carboxylate/sulfonate group to enzyme features.

    Conclusions:

    • The study provides detailed structural insights into beta-lactam antibiotic inhibition of bacterial DD-peptidase.
    • The findings highlight the importance of specific molecular interactions for antibiotic efficacy and stability.
    • This structural information can guide the design of more effective beta-lactam antibiotics.