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

ABSTRACT: The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 from Pseudomonas sp. strain AAC makes up half of a bicistronic operon responsible for ?-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.

SUBMITTER: Wilding M

PROVIDER: S-EPMC5287376 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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

Wilding Matthew M Scott Colin C Peat Thomas S TS Newman Janet J

Acta crystallographica. Section F, Structural biology communications 20170101 Pt 1

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 ...[more]

PMID: 28045390

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