6T3T
Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV
Summary for 6T3T
| Entry DOI | 10.2210/pdb6t3t/pdb |
| Descriptor | 4-hydroxy-tetrahydrodipicolinate synthase, SULFATE ION (3 entities in total) |
| Functional Keywords | thermoacidophile, methanotrophy, lysine biosynthesis, lyase |
| Biological source | Methylacidiphilum fumariolicum SolV |
| Total number of polymer chains | 4 |
| Total formula weight | 132728.99 |
| Authors | Schmitz, R.,Dietl, A.,Mueller, M.,Berben, T.,Op den Camp, H.,Barends, T. (deposition date: 2019-10-11, release date: 2020-05-06, Last modification date: 2024-01-24) |
| Primary citation | Schmitz, R.A.,Dietl, A.,Muller, M.,Berben, T.,Op den Camp, H.J.M.,Barends, T.R.M. Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway. Acta Crystallogr.,Sect.F, 76:199-208, 2020 Cited by PubMed 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. PubMed: 32356521DOI: 10.1107/S2053230X20005294 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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