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Structure paper

TitleCo-expression with chaperones can affect protein 3D structure as exemplified by loss-of-function variants of human prolidase.
Journal, issue, pagesFebs Lett., Vol. 594, Page 3045-3056, Year 2020
Publish dateSep 5, 2019 (structure data deposition date)
AuthorsWator, E. / Rutkiewicz, M. / Weiss, M.S. / Wilk, P.
External linksFebs Lett. / PubMed:32598484
MethodsX-ray diffraction
Resolution1.39 - 2.558 Å
Structure data

PDB-6sre:
Crystal Structure of Human Prolidase S202F variant expressed in the presence of chaperones
Method: X-RAY DIFFRACTION / Resolution: 1.39 Å

PDB-6srf:
Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones
Method: X-RAY DIFFRACTION / Resolution: 1.847 Å

PDB-6srg:
Crystal Structure of Human Prolidase G448R variant expressed in the presence of chaperones
Method: X-RAY DIFFRACTION / Resolution: 2.558 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-MH2:
MANGANESE ION, 1 HYDROXYL COORDINATED

ChemComp-GLY:
GLYCINE

ChemComp-PRO:
PROLINE

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-OH:
HYDROXIDE ION

Source
  • homo sapiens (human)
KeywordsHYDROLASE / prolidase / metallopeptidase / pathological variant / dipeptidase / metallohydrolase / pathological variants / metalloprotease

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