Structures of a γ-aminobutyrate (GABA) transaminase from the s-triazine-degrading organism Arthrobacter aurescens TC1 in complex with PLP and with its external aldimine PLP-GABA adduct.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 10): 1175-80, 2012 Oct 01.
Article
in En
| MEDLINE
| ID: mdl-23027742
ABSTRACT
Two complex structures of the γ-aminobutyrate (GABA) transaminase A1R958 from Arthrobacter aurescens TC1 are presented. The first, determined to a resolution of 2.80â
Å, features the internal aldimine formed by reaction between the â-amino group of Lys295 and the cofactor pyridoxal phosphate (PLP); the second, determined to a resolution of 2.75â
Å, features the external aldimine adduct formed between PLP and GABA in the first half-reaction. This is the first structure of a microbial GABA transaminase in complex with its natural external aldimine and reveals the molecular determinants of GABA binding in this enzyme.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arthrobacter
/
Pyridoxal Phosphate
/
4-Aminobutyrate Transaminase
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2012
Type:
Article
Affiliation country:
United kingdom