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Structure paper

TitleIron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.
Journal, issue, pagesProtein Sci., Vol. 32, Page e4788-e4788, Year 2023
Publish dateOct 14, 2022 (structure data deposition date)
AuthorsGabler, T. / Dali, A. / Sebastiani, F. / Furtmuller, P.G. / Becucci, M. / Hofbauer, S. / Smulevich, G.
External linksProtein Sci. / PubMed:37743577
MethodsX-ray diffraction
Resolution2.1 - 2.19 Å
Structure data

PDB-8bbv:
Coproporphyrin III - LmCpfC complex soaked 2min with Fe2+
Method: X-RAY DIFFRACTION / Resolution: 2.19 Å

PDB-8ofl:
Coproporphyrin III - LmCpfC complex soaked 4min with Fe2+
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-8omm:
Coproporphyrin III - LmCpfC complex soaked 3min with Fe2+
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HT9:
coproporphyrin III

ChemComp-FE2:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-MG:
Unknown entry

Source
  • listeria monocytogenes (bacteria)
KeywordsMETAL BINDING PROTEIN / ferrochelatase activity metal ion binding heme b biosynthesis / heme biosynthesis / coproporphyrin III / iron insertion / Ferrochelatase / Monomere / Heme b / Biosynthesis

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