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.
|Number of pages||5|
|Journal||Acta Crystallographica. Section F: Structural Biology Communications|
|Publication status||Published - 1 Jan 2017|
- Malonate-semialdehyde dehydrogenase
- Pseudomonas sp. strain AAC
- β-alanine catabolism