A high-affinity metal-binding peptide from Escherichia coli HypB.
The high-affinity nickel-binding site of the Escherichia coli [NiFe]-hydrogenase accessory protein HypB was localized to residues at the immediate N-terminus of the protein. Modification of a metal-binding fusion protein, site-directed mutagenesis experiments, and DFT calculations were used to identify the N-terminal amine as a ligand as well as the three cysteine residues in the CXXCGCXXX motif. This sequence can be removed from the protein and both a synthesized peptide and a protein fusion bind nickel with a similar affinity and the same structure as the parent metalloprotein, indicating the self-sufficiency of this high-affinity nickel-binding sequence.
Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6.
Kim C Chan
KC
Chung
Li
L
Cao
Alistair V
AV
Dias
Ingrid J
IJ
Pickering
Graham N
GN
George
Deborah B
DB
Zamble
D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D019204:GTP-Binding Proteins / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C089637:HypB protein, bacteria; D008024:Ligands; D010455:Peptides; D009532:Nickel; D019204:GTP-Binding Proteins