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Structure paper

TitleEvolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.
Journal, issue, pagesNature, Vol. 485, Page 530-533, Year 2012
Publish dateFeb 9, 2012 (structure data deposition date)
AuthorsNgaki, M.N. / Louie, G.V. / Philippe, R.N. / Manning, G. / Pojer, F. / Bowman, M.E. / Li, L. / Larsen, E. / Wurtele, E.S. / Noel, J.P.
External linksNature / PubMed:22622584
MethodsX-ray diffraction
Resolution1.55 - 1.9 Å
Structure data

PDB-4doi:
Crystal structure of Arabidopsis thaliana chalcone isomerase At3g55120 (AtCHI)
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4dok:
Crystal structure of Arabidopsis thaliana chalcone-isomerase like protein At5g05270 (AtCHIL)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4dol:
Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520 (AtFAP3)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4doo:
Crystal structure of Arabidopsis thaliana fatty-acid binding protein At3g63170 (AtFAP1)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-NO3:
NITRATE ION

ChemComp-HOH:
WATER

ChemComp-CA:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-PLM:
PALMITIC ACID

ChemComp-DAO:
LAURIC ACID

ChemComp-K:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
KeywordsISOMERASE / chalcone-flavanone isomerase / chalcone-isomerase like protein / chalcone-isomerase like fold / fatty-acid binding

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