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  Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway

Schmitz, R. A., Dietl, A., Müller, M., Berben, T., Op den Camp, H. J. M., & Barends, T. R. M. (2020). Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 76(5), 199-208. doi:10.1107/s2053230x20005294.

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 Creators:
Schmitz, Rob A, Author
Dietl, Andreas1, Author              
Müller, Melanie1, Author              
Berben, Tom, Author
Op den Camp, Huub J. M., Author
Barends, Thomas R. M.1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: 4-hydroxy-tetrahydrodipicolinate synthase; Methylacidiphilum fumariolicum SolV; aminotransferase pathway; methanotroph
 Abstract: The enzyme 4-hydroxy-tetrahydrodipicolinate synthase (DapA) is involved in the production of lysine and precursor molecules for peptidoglycan synthesis. In a multistep reaction, DapA converts pyruvate and L-aspartate-4-semialdehyde to 4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid. In many organisms, lysine binds allosterically to DapA, causing negative feedback, thus making the enzyme an important regulatory component of the pathway. Here, the 2.1 Å resolution crystal structure of DapA from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV is reported. The enzyme crystallized as a contaminant of a protein preparation from native biomass. Genome analysis reveals that M. fumariolicum SolV utilizes the recently discovered aminotransferase pathway for lysine biosynthesis. Phylogenetic analyses of the genes involved in this pathway shed new light on the distribution of this pathway across the three domains of life.

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Language(s): eng - English
 Dates: 2020-02-202020-04-152020-04-282020-05-01
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Source Genre: Journal
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Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 76 (5) Sequence Number: - Start / End Page: 199 - 208 Identifier: ISSN: 1744-3091
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000017210_1