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Structure of a calcium-binding carp myogen.

C E Nockolds, R H Kretsinger, C J Coffee

Proceedings of the National Academy of Sciences of the United States of America

|March 1, 1972

Summary

Researchers determined the structure of carp muscle calcium-binding protein B, a parvalbumin. Its calcium-binding site and hydrophobic core reveal insights into protein function and evolutionary relationships.

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Area of Science:

Biochemistry
Structural Biology
Molecular Biophysics

Background:

Carp muscle contains three closely related parvalbumins.
Calcium-binding proteins play crucial roles in cellular processes.

Purpose of the Study:

To determine the amino acid sequence and 3D structure of carp muscle calcium-binding protein B.
To elucidate the calcium coordination site and structural features of this parvalbumin.

Main Methods:

X-ray crystallography with heavy-atom substitution.
Calculation of electron density map to 2.0-A resolution.

Main Results:

The structure reveals the orientation of amino acid side chains.
Calcium is coordinated by one glutamic and three aspartic acid residues in a tetrahedral arrangement.
The protein core is hydrophobic, with phenylalanine residues packed in a herringbone pattern.
52 of 108 residues form six alpha-helices; no beta-pleated sheet is present.
The N-terminal alanine is acetylated and likely solvent-inaccessible.
Heavy-atom derivatives bind to the single cysteine residue.

Conclusions:

The determined structure provides detailed insights into carp parvalbumin.
The calcium-binding site and hydrophobic core are key structural features.
The protein's properties suggest a relationship to mammalian troponin A.

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