Related Experiment Video

Updated: Jun 6, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

3.9K

Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori

Dylan E Davis1, Jesuferanmi P Ayanlade2, David T Laseinde2

  • 1College of Arts and Science, Dartmouth College, Hanover, NH 03755, USA.

Acta Crystallographica. Section F, Structural Biology Communications
|November 27, 2024
PubMed

Insights

Developing new treatments for Helicobacter pylori infection is crucial due to rising drug resistance. Researchers determined the structure of H. pylori Glutamyl-tRNA synthetase (HpGluRS), a potential drug target, revealing similarities to other bacterial enzymes for drug development.

Area of Science:

  • Microbiology
  • Structural Biology
  • Drug Discovery

Background:

  • Helicobacter pylori infection affects over two-thirds of the global population, leading to gastric ulcers and cancers.
  • Increasing antibiotic resistance necessitates the development of alternative therapeutic strategies against H. pylori.

Purpose of the Study:

  • To investigate Glutamyl-tRNA synthetase (GluRS) from H. pylori as a potential drug target.
  • To determine the apo structure of H. pylori GluRS (HpGluRS) for structure-function analysis.

Main Methods:

  • Production and crystallization of HpGluRS.
  • Determination of the apo structure of HpGluRS using X-ray crystallography.
  • Comparative analysis of HpGluRS structure with other bacterial GluRS enzymes.

Main Results:

  • The apo structure of HpGluRS was successfully determined.
  • HpGluRS exhibits a typical bacterial GluRS topology with conserved binding sites and tertiary structures.
  • Key residues for glutamate binding in HpGluRS are conserved compared to Pseudomonas aeruginosa GluRS (PaGluRS).

Conclusions:

  • HpGluRS is a viable drug target for developing new antibacterials.
  • Structural similarities between HpGluRS and PaGluRS can guide the design of novel inhibitors.
  • Exploiting these similarities may lead to effective treatments for H. pylori infections, reducing associated gastric diseases.

Keywords:
Seattle Structural Genomics Center for Infectious Diseasecancergastric ulcersglutamyl-tRNA synthetaseinfectious diseasesundergraduate education and training

More Related Videos

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase09:31

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase

Published on: September 26, 2020

4.3K
Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

7.4K

Related Concept Videos

tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
19.0K
Protein Organization01:13

Protein Organization

Overview
136.6K
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
78.5K
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
4.7K
Protein Folding01:22

Protein Folding

Overview
117.4K
Termination of Translation01:44

Termination of Translation

The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
25.0K