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TitleCharacterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1814, Page 1900-1909, Year 2011
Publish dateOct 19, 2010 (structure data deposition date)
AuthorsPearce, F.G. / Dobson, R.C. / Jameson, G.B. / Perugini, M.A. / Gerrard, J.A.
External linksBiochim. Biophys. Acta / PubMed:21803176
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-3pb0:
Characterisation of the first monomeric dihydrodipicolinate synthase variant reveals evolutionary insights
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3pb2:
Characterisation of the first monomeric dihydrodipicolinate synthase variant reveals evolutionary insights
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • thermotoga maritima (bacteria)
KeywordsLYASE / dihydrodipicolinate synthase / TIM-Barrel

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