 |
PDBsum entry 6t3t
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Structure of the 4-Hydroxy-Tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph methylacidiphilum fumariolicum solv and the phylogeny of the aminotransferase pathway.
|
|
|
Authors
|
|
R.A.Schmitz,
A.Dietl,
M.Müller,
T.Berben,
H.J.M.Op den camp,
T.R.M.Barends.
|
|
|
Ref.
|
|
Acta Crystallogr F Struct Biol Commun, 2020,
76,
199-208.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
