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Structure paper

TitleTryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF
Journal, issue, pagesJ. Biol. Inorg. Chem., Vol. 14, Page 905-912, Year 2009
Publish dateAug 17, 2008 (structure data deposition date)
AuthorsLoftin, I.R. / Blackburn, N.J. / McEvoy, M.M.
External linksJ. Biol. Inorg. Chem. / PubMed:19381697
MethodsX-ray diffraction
Resolution1 Å
Structure data

PDB-3e6z:
1.0 A Structure of CusF-W44A-Cu(II) residues 10-88 from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 1 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsMETAL BINDING PROTEIN / copper-binding / beta-barrel / OB-fold / metalloprotein / metal resistance / copper chaperone / Metal-binding / Periplasm

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