Crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC

Matthew Wilding, Colin Scott, Janet Newman, Thomas S. Peat*

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The putrescine aminotransferase KES24511 from Pseudomonas sp. strain AAC was previously identified as an industrially relevant enzyme based on the discovery that it is able to promiscuously catalyse the transamination of 12-aminododecanoic acid. Here, the cloning, heterologous expression, purification and successful crystallization of the KES24511 protein are reported, which ultimately generated crystals adopting space group I2. The crystals diffracted X-rays to 2.07 Å resolution and data were collected using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4a6t as the search model. The crystal structure of a putrescine aminotransferase from Pseudomonas sp. strain AAC has been determined to a resolution of 2.07 Å.

Original languageEnglish
Pages (from-to)29-35
Number of pages7
JournalActa Crystallographica. Section F: Structural Biology Communications
Volume73
Issue number1
DOIs
Publication statusPublished - 1 Jan 2017
Externally publishedYes

Keywords

  • 12-aminododecanoic acid
  • aminotransferases
  • PLP-dependent
  • transaminase

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