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Structure paper

TitleCrystallographic structure of recombinant Lactococcus lactis prolidase to support proposed structure-function relationships.
Journal, issue, pagesBiochim Biophys Acta Proteins Proteom, Vol. 1865, Page 473-480, Year 2017
Publish dateJun 30, 2020 (structure data deposition date)
AuthorsKgosisejo, O. / Chen, J.A. / Grochulski, P. / Tanaka, T.
External linksBiochim Biophys Acta Proteins Proteom / PubMed:28179139
MethodsX-ray diffraction
Resolution1.7 - 2.7 Å
Structure data

PDB-6xmr:
X-ray crystallographic structure model of Lactococcus lactis prolidase mutant H38S
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-7k3u:
X-ray crystallographic structure model of Lactococcus lactis prolidase mutant R293S
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-7n02:
X-ray crystallographic structure model of Lactococcus lactis prolidase mutant D36S
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • lactococcus lactis (lactic acid bacteria)
KeywordsHYDROLASE / proline-specific / allosteric behaviour / substrate inhibition / dipeptidase / lactic acid bacteria / debittering of fermented foods

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