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TitleCharacterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.
Journal, issue, pagesNat Commun, Vol. 8, Page 1045-1045, Year 2017
Publish dateFeb 10, 2017 (structure data deposition date)
AuthorsCzekster, C.M. / Ludewig, H. / McMahon, S.A. / Naismith, J.H.
External linksNat Commun / PubMed:29051530
MethodsX-ray diffraction
Resolution1.44 - 2.9 Å
Structure data

PDB-5n4b:
Prolyl oligopeptidase B from Galerina marginata bound to 25mer macrocyclization substrate - S577A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-5n4c:
Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - S577A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-5n4d:
Prolyl oligopeptidase B from Galerina marginata bound to 25mer macrocyclization substrate - D661A mutant
Method: X-RAY DIFFRACTION / Resolution: 1.62 Å

PDB-5n4e:
Prolyl oligopeptidase B from Galerina marginata bound to 35mer hydrolysis and macrocyclization substrate - H698A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-5n4f:
Prolyl oligopeptidase B from Galerina marginata - apo protein
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

Source
  • galerina marginata (funeral bell)
KeywordsHYDROLASE / amanitin biosynthesis / prolyl oligopeptidase / macrocyclase / peptidase / beta-propeller / closed form / open form

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