| Title | Crystal structure of Dihydrodipicolinate synthase (TM1521) from Thermotoga maritima at 1.80 A resolution. To be published | | Site | JCSG | | PDB Id | | Target Id | 283378 | | Molecular Characteristics | | Source | Thermotoga maritima msb8 | | Alias Ids | TPS1296,TM1521 | Molecular Weight | 32388.59 Da. | | Residues | 294 | Isoelectric Point | 5.91 | | Sequence | mfrgvgtaivtpfkngeldlesyerlvryqlengvnalivlgttgesptvnedereklvsrtleivdgk ipvivgagtnstektlklvkqaeklgangvlvvtpyynkptqeglyqhykyisertdlgivvynvpgrt gvnvlpetaariaadlknvvgikeanpdidqidrtvsltkqarsdfmvwsgnddrtfyllcaggdgvis vvsnvapkqmvelcaeyfsgnleksrevhrklrplmkalfvetnpipvkaalnlmgfienelrlplvpa sektvellrnvlkesgll | | | BLAST FFAS | | Structure Determination | | Method | XRAY | Chains | 2 | | Resolution (Å) | 1.80 | Rfree | 0.18593 | | Matthews' coefficent | 2.12 | Rfactor | 0.13941 | | Waters | 508 | Solvent Content | 41.42 |
| Pathway | | Reactions found in Metabolic Reconstruction for TM1521 | Name: dihydrodipicolinate synthase
Metabolic Subsystem: Lysine Biosynthesis
Reaction: :
aspsa
Name:L-Aspartate 4-semialdehyde
Formula:C4H7NO3
KEGG:
C00441
+
pyr
Name:Pyruvate
Formula:C3H3O3
KEGG:
C00022
-->
23dhdp
Name:"2,3-Dihydrodipicolinate"
Formula:C7H5NO4
KEGG:
C03340
+
h
Name:H+
Formula:H
KEGG:
C00080
+
h2o
Name:H2O
Formula:H2O
KEGG:
C00001
Classification: EC:4.2.1.52
|
| Ligand Information | | Ligands | | | Metals | | | |
Protein Summary
The gene TM1521 from Thermotoga maritima encodes dihydrodipicolinate synthase, a DHDPS enzyme superfamily PF00701 COG0329. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways. The other name of the enzyme is N-acetylneuraminate lyase. DHDPS is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta-semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a conserved lysine residue [Ref]. The functional enzyme is a homotetramer consisting of a dimer of dimers. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)-lysine. The structure of E.coli homologue and its multiple mutant forms have been previously solved 1S5W, 2A6N.
Ligand Summary
References
