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TitleA d-pathway mutation decouples the paracoccusdenitrificans cytochrome C oxidase by altering the side-chain orientation of a distant conserved glutamate.
Journal, issue, pagesJ. Mol. Biol., Vol. 384, Page 865-877, Year 2008
Publish dateSep 12, 2008 (structure data deposition date)
AuthorsDurr, K.L. / Koepke, J. / Hellwig, P. / Muller, H. / Angerer, H. / Peng, G. / Olkhova, E. / Richter, O.-M.H. / Ludwig, B. / Michel, H.
External linksJ. Mol. Biol. / PubMed:18930738
MethodsX-ray diffraction
Resolution2.32 Å
Structure data

PDB-3ehb:
A D-Pathway Mutation Decouples the Paracoccus Denitrificans Cytochrome c Oxidase by Altering the side chain orientation of a distant, conserved Glutamate
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

Chemicals

ChemComp-HEA:
HEME-A

ChemComp-CU:
COPPER (II) ION

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-LDA:
LAURYL DIMETHYLAMINE-N-OXIDE / LDAO, detergent*YM

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-PER:
PEROXIDE ION

ChemComp-HOH:
WATER

Source
  • paracoccus denitrificans (bacteria)
  • mus musculus (house mouse)
KeywordsOXIDOREDUCTASE/IMMUNE SYSTEM / proton pumping / water chain / electron transfer / Cell inner membrane / Cell membrane / Copper / Electron transport / Heme / Hydrogen ion transport / Ion transport / Iron / Membrane / Metal-binding / Oxidoreductase / Respiratory chain / Transmembrane / Transport / Pyrrolidone carboxylic acid / OXIDOREDUCTASE-IMMUNE SYSTEM COMPLEX

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