Structure of subunit I of the anthranilate synthase complex of Mycolicibacterium smegmatis.
Biochem Biophys Res Commun
; 527(1): 37-41, 2020 06 18.
Article
in En
| MEDLINE
| ID: mdl-32446388
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Mycobacterium smegmatis
/
Anthranilate Synthase
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2020
Document type:
Article
Affiliation country:
China