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Structure paper

TitleHow Periplasmic Thioredoxin TlpA Reduces Bacterial Copper Chaperone ScoI and Cytochrome Oxidase Subunit II (CoxB) Prior to Metallation.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 32431-32444, Year 2014
Publish dateJul 4, 2014 (structure data deposition date)
AuthorsAbicht, H.K. / Scharer, M.A. / Quade, N. / Ledermann, R. / Mohorko, E. / Capitani, G. / Hennecke, H. / Glockshuber, R.
External linksJ. Biol. Chem. / PubMed:25274631
MethodsX-ray diffraction
Resolution2 - 2.2 Å
Structure data

PDB-4txo:
Crystal structure of the mixed disulfide complex of thioredoxin-like TlpAs(C110S) and copper chaperone ScoIs(C74S)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-4txv:
Crystal structure of the mixed disulfide intermediate between thioredoxin-like TlpAs(C110S) and subunit II of cytochrome c oxidase CoxBPD (C233S)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SCN:
THIOCYANATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bradyrhizobium diazoefficiens usda 110 (bacteria)
  • bradyrhizobium diazoefficiens (bacteria)
  • bradyrhizobium diazoefficiens (strain jcm 10833 / iam 13628 / nbrc 14792 / usda 110) (bacteria)
KeywordsOXIDODREDUCTASE/COPPER BINDING PROTEIN / mixed disulfide / soluble domain of membrane protein / thioredoxin fold / copper protein / protein binding / OXIDODREDUCTASE-COPPER BINDING PROTEIN complex / thioredoxin / mixed disulphide / cytochrome c oxidase

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