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Structure paper

TitleCrystal structure and biochemical investigations reveal novel mode of substrate selectivity and illuminate substrate inhibition and allostericity in a subfamily of Xaa-Pro dipeptidases.
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1865, Page 153-164, Year 2017
Publish dateDec 15, 2015 (structure data deposition date)
AuthorsAre, V.N. / Kumar, A. / Kumar, S. / Goyal, V.D. / Ghosh, B. / Bhatnagar, D. / Jamdar, S.N. / Makde, R.D.
External linksBiochim. Biophys. Acta / PubMed:27816563
MethodsX-ray diffraction
Resolution1.85 - 1.95 Å
Structure data

PDB-5fcf:
Crystal Structure of Xaa-Pro dipeptidase from Xanthomonas campestris, phosphate and Mn bound
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5fch:
Crystal Structure of Xaa-Pro dipeptidase from Xanthomonas campestris, phosphate and Zn bound
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • xanthomonas campestris pv. campestris str. atcc 33913 (bacteria)
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Xaa-pro dipeptidase / prolidase / M24 family / phosphate

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