Amino acid sequence of the blue copper protein rusticyanin from Thiobacillus ferrooxidans

Rusticyanin is a small blue copper protein isolated from Thiobacillus ferrooxidans. The amino acid sequence of the rusticyanin has been determined by the structural characterization of tryptic and endoproteinase Asp-N peptides with use of amino terminal microsequencing, fast atom bombardment mass sp...

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Bibliographic Details
Published in:Biochemistry (Easton) 1991-10, Vol.30 (39), p.9435-9442
Main Authors: Ronk, Michael, Shively, John E, Shute, Elizabeth A, Blake, Robert C
Format: Article
Language:English
Subjects:
550200 - Biochemistry
AMINO ACID SEQUENCE
AMINO ACIDS
Amino Acids - analysis
ASPARTIC ACID
Azurin - analogs & derivatives
Azurin - chemistry
BACILLUS
BACTERIA
Bacterial Proteins - chemistry
BASIC BIOLOGICAL SCIENCES
CARBOXYLIC ACIDS
Circular Dichroism
DICHROISM
ELEMENTS
EXTRACTION
MAGNETIC CIRCULAR DICHROISM
Mass Spectrometry
MASS SPECTROSCOPY
METALLOPROTEINS
METALS
MICROORGANISMS
Molecular Sequence Data
MOLECULAR STRUCTURE
ORGANIC ACIDS
ORGANIC COMPOUNDS
Peptide Mapping
Peptides - chemistry
Protein Conformation
PROTEINS
SEPARATION PROCESSES
Sequence Alignment
SPECTROSCOPY
STRUCTURAL MODELS
SULFUR-OXIDIZING BACTERIA
Thiobacillus - analysis
Thiobacillus ferrooxidans
THIOBACILLUS FERROXIDANS
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Description
Summary:Rusticyanin is a small blue copper protein isolated from Thiobacillus ferrooxidans. The amino acid sequence of the rusticyanin has been determined by the structural characterization of tryptic and endoproteinase Asp-N peptides with use of amino terminal microsequencing, fast atom bombardment mass spectrometry, and electrospray triple-quadrupole mass spectrometry techniques. Amino acid analysis, carboxy-terminal sequence analysis, and circular dichroism spectroscopy were also performed on the protein. Amino acid sequence identity among rusticyanin and six other small blue copper proteins is apparent only in the limited C-terminal region of each protein bearing three of the four putative copper ligands. A structural model of the rusticyanin is proposed where the protein is principally a beta-barrel comprised of six strands. This model is consistent with the circular dichroism data and computational predictions of the secondary structure of rusticyanin. A feature of the model is the hypothesis that Asp 73 may serve as a fourth copper ligand.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00103a007