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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

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Author(s)

  • H. Bruce
  • A. Nguyen Tuan
  • C. Leese
  • R. Hyde
  • S. Hart
  • J.P. Turkenburg
  • G. Grogan
  • J. Mangas Sánchez
  • J. Hopwood

Department/unit(s)

Publication details

JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
DatePublished - 1 Oct 2012
Issue number10
Volume68
Pages (from-to)1175-1180
Original languageEnglish

Abstract

Two complex structures of the γ-aminobutyrate (GABA) transaminase A1R958 from Arthrobacter aurescens TC1 are presented. The first, determined to a resolution of 2.80 Å, 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 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.

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