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TitlePeptide deformylases from Vibrio parahaemolyticus phage and bacteria display similar deformylase activity and inhibitor binding clefts.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1866, Page 348-355, Year 2018
Publish dateJan 9, 2017 (structure data deposition date)
AuthorsGrzela, R. / Nusbaum, J. / Fieulaine, S. / Lavecchia, F. / Desmadril, M. / Nhiri, N. / Van Dorsselaer, A. / Cianferani, S. / Jacquet, E. / Meinnel, T. / Giglione, C.
External linksBiochim. Biophys. Acta / PubMed:29101077
MethodsX-ray diffraction
Resolution1.4 Å
Structure data

PDB-5mte:
Crystal structure of PDF from the Vibrio parahaemolyticus bacteriophage VP16T in complex with actinonin - crystal form II
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-BB2:
ACTINONIN / antitumor, antibiotic*YM

ChemComp-ZN:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

Source
  • vibrio phage vp16t (virus)
KeywordsHYDROLASE / PDF / peptide deformylase / type 1B / bacteriophage VP16T / actinonin

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