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Structure paper

TitlePlant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.
Journal, issue, pagesBiochem. J., Vol. 475, Page 137-150, Year 2018
Publish dateDec 6, 2016 (structure data deposition date)
AuthorsWatkin, S.A.J. / Keown, J.R. / Richards, E. / Goldstone, D.C. / Devenish, S.R.A. / Grant Pearce, F.
External linksBiochem. J. / PubMed:29187521
MethodsX-ray diffraction
Resolution2.1 - 2.7 Å
Structure data

PDB-5u5i:
The dimeric crystal structure of the selenomethionine derivative of HTPA Reductase from Sellaginella moellendorffii
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-5u5n:
The dimeric crystal structure of HTPA Reductase from Sellaginella moellendorffii
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-5ua0:
Dimeric crystal structure of HTPA reductase from arabidopsis thaliana
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-5ugj:
Crystal structure of HTPA Reductase from neisseria meningitidis
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • selaginella moellendorffii (plant)
  • arabidopsis thaliana (thale cress)
  • neisseria meningitidis serogroup b (strain mc58) (bacteria)
KeywordsOXIDOREDUCTASE / DHDPR / Dihydrodipicolinate reductase / HTPA reductase / HTPA Reductase DHDPR Lysine biosynthesis / HTPA Reductase Lysine biosynthesis DHDPR

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