X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC

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

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 from Pseudomonas sp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space group P212121 and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model. The crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC has been determined to a nominal resolution of 2.95 Å.

Original languageEnglish
Pages (from-to)24-28
Number of pages5
JournalActa Crystallographica Section:F Structural Biology Communications
Volume73
Issue number1
DOIs
Publication statusPublished - 1 Jan 2017
Externally publishedYes

Keywords

  • Malonate-semialdehyde dehydrogenase
  • Pseudomonas sp. strain AAC
  • β-alanine catabolism

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