Related Experiment Video
Updated: Dec 20, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
Published on: September 14, 2014
Structure of subunit I of the anthranilate synthase complex of Mycolicibacterium smegmatis
Yujing Chen1, Haizhu Jia1, Ruihua Liu2
1College of Life Sciences, Nankai University, Tianjin, 300071, China.
Abstract:
The tryptophan biosynthesis pathway, which does not exist in mammals, is highly conserved in Mycobacterium. Anthranilate synthase (AS) catalyzes the initial reactions in the tryptophan biosynthesis pathway in many microorganisms, catalyzing the conversion of glutamine and chorismate to form pyruvate and anthranilate. Here, the crystal structure of anthranilate synthase component I (AS I) from Mycolicibacterium smegmatis (MsTrpE) has been determined to 1.7 Å resolution. MsTrpE crystallizes in the space group P1 with two monomers in the asymmetric unit, which is consistent with the oligomeric state in solution as confirmed by analytical ultracentrifugation. Inspection of the active site shows that it is in the active form with a bound Mg2+ ion and a ligand that is modelled as benzoate. The position of benzoate mimics the position of the anthranilate product in the active site. The structure of MsTrpE will provide a starting point for the investigation of latent biotechnology and pharmaceutical applications of anthranilate synthase component I.
More Related Videos
10:01Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
11:55In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
Published on: October 10, 2014
Related Concept Videos
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Electron Transport Chain: Complex III and IV
The Supercomplexes in the Crista Membrane
ATP Synthase: Mechanism
The Antenna Complex
ATP Synthase: Structure