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Structure paper

TitleActinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation.
Journal, issue, pagesAcs Catalysis, Vol. 10, Page 5405-5418, Year 2020
Publish dateJan 17, 2020 (structure data deposition date)
AuthorsMichlits, H. / Lier, B. / Pfanzagl, V. / Djinovic-Carugo, K. / Furtmuller, P.G. / Oostenbrink, C. / Obinger, C. / Hofbauer, S.
External linksAcs Catalysis / PubMed:32440366
MethodsX-ray diffraction
Resolution1.78 - 1.8702 Å
Structure data

PDB-6xub:
Structure of coproheme decarboxylase from Corynebacterium diphteriae in complex with monovinyl monopropionyl deuteroheme
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-6xuc:
Structure of coproheme decarboxylase from Corynebacterium diphteriae in complex with coproheme
Method: X-RAY DIFFRACTION / Resolution: 1.8702 Å

Chemicals

ChemComp-VOV:
harderoheme (III)

ChemComp-HOH:
WATER

ChemComp-FEC:
1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX

Source
  • corynebacterium diphtheriae (bacteria)
KeywordsOXIDOREDUCTASE / Coproheme decarboxylase / heme b biosynthesis / decarboxylation / ferredoxin like / actinobacterial

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