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

Matthew Wilding; Colin Scott; Thomas S. Peat; Janet Newman

doi:10.1107/S2053230X16020008

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

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

Research output: Contribution to journal › Article › peer-review

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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 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 language	English
Pages (from-to)	24-28
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	73
Issue number	1
DOIs	https://doi.org/10.1107/S2053230X16020008
Publication status	Published - 1 Jan 2017
Externally published	Yes

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title = "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 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 {\AA} 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 {\AA}.",

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author = "Matthew Wilding and Colin Scott and Peat, {Thomas S.} and Janet Newman",

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T1 - X-ray crystal structure of a malonate-semialdehyde dehydrogenase from Pseudomonas sp. strain AAC

AU - Wilding, Matthew

AU - Scott, Colin

AU - Peat, Thomas S.

AU - Newman, Janet

PY - 2017/1/1

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AB - 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.

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KW - Pseudomonas sp. strain AAC

KW - β-alanine catabolism

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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IS - 1

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

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