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

假单胞菌属AAC菌株丙二酸半醛脱氢酶的X射线晶体结构

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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 P2(1)2(1)2(1) 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.

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