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TitleHigh-resolution structure of a lytic polysaccharide monooxygenase from Hypocrea jecorina reveals a predicted linker as an integral part of the catalytic domain.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 19099-19109, Year 2017
Publish dateMay 23, 2017 (structure data deposition date)
AuthorsHansson, H. / Karkehabadi, S. / Mikkelsen, N. / Douglas, N.R. / Kim, S. / Lam, A. / Kaper, T. / Kelemen, B. / Meier, K.K. / Jones, S.M. ...Hansson, H. / Karkehabadi, S. / Mikkelsen, N. / Douglas, N.R. / Kim, S. / Lam, A. / Kaper, T. / Kelemen, B. / Meier, K.K. / Jones, S.M. / Solomon, E.I. / Sandgren, M.
External linksJ. Biol. Chem. / PubMed:28900033
MethodsX-ray diffraction
Resolution0.95 - 2 Å
Structure data

PDB-5o2w:
Extended catalytic domain of Hypocrea jecorina LPMO 9A.
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5o2x:
Extended catalytic domain of H. jecorina LPMO9A a.k.a EG4
Method: X-RAY DIFFRACTION / Resolution: 0.95 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-CU:
COPPER (II) ION

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • trichoderma reesei qm6a (fungus)
KeywordsOXIDOREDUCTASE / Metalloprotein / Lytic polysaccharide monooxygenase Trichoderma reesei EG4

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