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Structure paper

TitleStructure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 8244-8261, Year 2017
Publish dateNov 17, 2016 (structure data deposition date)
AuthorsGrishkovskaya, I. / Paumann-Page, M. / Tscheliessnig, R. / Stampler, J. / Hofbauer, S. / Soudi, M. / Sevcnikar, B. / Oostenbrink, C. / Furtmuller, P.G. / Djinovic-Carugo, K. ...Grishkovskaya, I. / Paumann-Page, M. / Tscheliessnig, R. / Stampler, J. / Hofbauer, S. / Soudi, M. / Sevcnikar, B. / Oostenbrink, C. / Furtmuller, P.G. / Djinovic-Carugo, K. / Nauseef, W.M. / Obinger, C.
External linksJ. Biol. Chem. / PubMed:28348079
MethodsX-ray diffraction
Resolution1.2 Å
Structure data

PDB-5mfa:
Crystal structure of human promyeloperoxidase (proMPO)
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

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

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / Myeloperoxidase / proMPO / biosynthesis / proteolytic maturation / halide oxidation

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