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TitleThe C-terminal residue of phage Vp16 PDF, the smallest peptide deformylase, acts as an offset element locking the active conformation.
Journal, issue, pagesSci Rep, Vol. 7, Page 11041-11041, Year 2017
Publish dateJan 9, 2017 (structure data deposition date)
AuthorsGrzela, R. / Nusbaum, J. / Fieulaine, S. / Lavecchia, F. / Bienvenut, W.V. / Dian, C. / Meinnel, T. / Giglione, C.
External linksSci Rep / PubMed:28887476
MethodsX-ray diffraction
Resolution1.5 - 1.7 Å
Structure data

PDB-5mtc:
Crystal structure of PDF from the Vibrio parahaemolyticus bacteriophage VP16T - crystal form I
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-5mtd:
Crystal structure of PDF from the Vibrio parahaemolyticus bacteriophage VP16T - crystal form II
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

ChemComp-PGE:
TRIETHYLENE GLYCOL

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

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