Structural highlights
Function
A1R958_PAEAT
Publication Abstract from PubMed
Two complex structures of the gamma-aminobutyrate (GABA) transaminase A1R958 from Arthrobacter aurescens TC1 are presented. The first, determined to a resolution of 2.80 A, features the internal aldimine formed by reaction between the -amino group of Lys295 and the cofactor pyridoxal phosphate (PLP); the second, determined to a resolution of 2.75 A, 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.
Structures of a gamma-aminobutyrate (GABA) transaminase from the s-triazine-degrading organism Arthrobacter aurescens TC1 in complex with PLP and with its external aldimine PLP-GABA adduct.,Bruce H, Nguyen Tuan A, Mangas Sanchez J, Leese C, Hopwood J, Hyde R, Hart S, Turkenburg JP, Grogan G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1175-80., doi: 10.1107/S1744309112030023. Epub 2012 Sep 29. PMID:23027742[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bruce H, Nguyen Tuan A, Mangas Sanchez J, Leese C, Hopwood J, Hyde R, Hart S, Turkenburg JP, Grogan G. Structures of a gamma-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. 2012 Oct 1;68(Pt 10):1175-80., doi: 10.1107/S1744309112030023. Epub 2012 Sep 29. PMID:23027742 doi:http://dx.doi.org/10.1107/S1744309112030023
