A High-Affinity Metal-Binding Peptide From Escherichia Coli Hypb

Journal Article · Tue May 12 04:00:00 EDT 2009 · J. Am. Chem. Soc. 130:14056,2008

OSTI ID:958594

Chung, K C Chan; Cao, L; Dias, A V; Pickering, I J; George, G N; Zamble, D B

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.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 958594
• Report Number(s): SLAC-REPRINT-2009-095
• Journal Information: J. Am. Chem. Soc. 130:14056,2008, Journal Name: J. Am. Chem. Soc. 130:14056,2008 Journal Issue: 43 Vol. 130; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
AFFINITY
AMINES
CYSTEINE
ESCHERICHIA COLI
MODIFICATIONS
MUTAGENESIS
NICKEL
Other
CHEM
PEPTIDES
PROTEINS
RESIDUES