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TitleEvolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 25708-25719, Year 2010
Publish dateMay 17, 2010 (structure data deposition date)
AuthorsDeng, X. / Lee, J. / Michael, A.J. / Tomchick, D.R. / Goldsmith, E.J. / Phillips, M.A.
External linksJ. Biol. Chem. / PubMed:20534592
MethodsX-ray diffraction
Resolution1.9 - 2.3 Å
Structure data

PDB-3n29:
Crystal structure of carboxynorspermidine decarboxylase complexed with Norspermidine from Campylobacter jejuni
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3n2o:
X-ray crystal structure of arginine decarboxylase complexed with Arginine from Vibrio vulnificus
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-NSD:
N-(3-aminopropyl)propane-1,3-diamine / medication*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-AG2:
AGMATINE

Source
  • campylobacter jejuni subsp. jejuni 81116 (Campylobacter)
  • vibrio vulnificus (bacteria)
KeywordsLYASE

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