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Structure paper

TitleUnderstanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 242-252, Year 2014
Publish dateFeb 26, 2013 (structure data deposition date)
AuthorsFieulaine, S. / Desmadril, M. / Meinnel, T. / Giglione, C.
External linksActa Crystallogr. ,Sect. D / PubMed:24531459
MethodsX-ray diffraction
Resolution2 - 2.4 Å
Structure data

PDB-4je6:
Crystal structure of a human-like mitochondrial peptide deformylase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-4je7:
Crystal structure of a human-like mitochondrial peptide deformylase in complex with actinonin
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4je8:
Crystal structure of a human-like mitochondrial peptide deformylase in complex with Met-Ala-Ser
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-BB2:
ACTINONIN / antitumor, antibiotic*YM

Source
  • arabidopsis thaliana (thale cress)
KeywordsHYDROLASE / peptide deformylase / mitochondrial / HYDROLASE/HYDROLASE INHIBITOR / actinonin / HYDROLASE-HYDROLASE INHIBITOR complex / HYDROLASE/PEPTIDE / HYDROLASE-PEPTIDE complex

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