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Structure paper

TitleHow essential is the 'essential' active-site lysine in dihydrodipicolinate synthase?
Journal, issue, pagesBiochimie, Vol. 92, Page 837-845, Year 2010
Publish dateJul 8, 2009 (structure data deposition date)
AuthorsSoares da Costa, T.P. / Muscroft-Taylor, A.C. / Dobson, R.C. / Devenish, S.R. / Jameson, G.B. / Gerrard, J.A.
External linksBiochimie / PubMed:20353808
MethodsX-ray diffraction
Resolution2 - 2.3 Å
Structure data

PDB-3i7q:
Dihydrodipicolinate synthase mutant - K161A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3i7r:
Dihydrodipicolinate synthase - K161R
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3i7s:
Dihydrodipicolinate synthase mutant - K161A - with the substrate pyruvate bound in the active site.
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-K:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-PYR:
PYRUVIC ACID

Source
  • escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsLYASE / dihydrodipicolinate synthase / lysine biosynthesis / Amino-acid biosynthesis / Diaminopimelate biosynthesis / Schiff base / dihydrodipicolinate synthyase

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