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Related Experiment Video

Updated: Jun 7, 2026

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes

Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes

Published on: December 19, 2020

The homodimeric GBS1074 from Streptococcus agalactiae.

Anshuman Shukla¹, Mark Pallen, Mark Anthony

¹School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, England.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

|November 4, 2010

Summary

The crystal structure of Streptococcus agalactiae

Area of Science:

Microbiology
Structural Biology
Protein Crystallography

Background:

ESAT-6 is a secreted protein from Mycobacterium tuberculosis and the archetype of the WXG100 protein family.
Homologues of ESAT-6 have been found in Streptococcus agalactiae, a human pathogen.
The esxA gene encoding one such homologue was cloned and the recombinant protein crystallized.

Purpose of the Study:

To determine the crystal structure of the Streptococcus agalactiae ESAT-6 homologue, GBS1074.
To compare the structure of GBS1074 with other known ESAT-6 family proteins.

Main Methods:

Gene cloning and recombinant protein expression.
Protein crystallization.
X-ray crystallography to determine the 3D structure.

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Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG

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Published on: May 16, 2017

Main Results:

The crystal structure of GBS1074 was determined.
GBS1074 adopts a homodimeric structure, similar to homologous proteins from Staphylococcus aureus and Helicobacter pylori.
Uniquely, GBS1074 forms elongated, fiber-like assemblies in the crystal structure.

Conclusions:

The crystal structure of GBS1074 reveals structural similarities and differences compared to Mycobacterium tuberculosis ESAT-6.
The observed fiber-like assemblies suggest potential novel biological functions or interactions of GBS1074.