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TitleStructural and functional studies of histidine biosynthesis in Acanthamoeba spp. demonstrates a novel molecular arrangement and target for antimicrobials.
Journal, issue, pagesPLoS ONE, Vol. 13, Page e0198827-e0198827, Year 2018
Publish dateMar 6, 2018 (structure data deposition date)
AuthorsRice, C.A. / Campbell, S.J. / Bisson, C. / Owen, H.J. / Sedelnikova, S.E. / Baker, P.J. / Rice, D.W. / Henriquez, F.L. / Roberts, C.W.
External linksPLoS ONE / PubMed:29969448
MethodsX-ray diffraction
Resolution1.79 Å
Structure data

PDB-6fwh:
Acanthamoeba IGPD in complex with R-C348 to 1.7A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-5LD:
[(2R)-2-hydroxy-3-(1H-1,2,4-triazol-1-yl)propyl]phosphonic acid

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • acanthamoeba castellanii (eukaryote)
KeywordsLYASE / Inhibitor / Histidine biosynthesis / Acanthamoeba

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