Structure of a Calcium-Binding Carp Myogen
- 1 March 1972
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 69 (3), 581-584
- https://doi.org/10.1073/pnas.69.3.581
Abstract
The amino-acid sequence and three-dimensional structure of a calcium-binding protein prepared from carp muscle has been determined. This protein, designated carp-muscle calcium-binding protein B, is one of three closely related parvalbumins found in this tissue. The electron density map, calculated by heavyatom substitution crystallographic methods to 2.0-A resolution, reveals the orientation of most of the amino-acid side chains. The calcium coordination site consists of one glutamic- and three aspartic-acid carboxyl groups in a tetrahedral arrangement. The core of this spherical molecule is remarkably hydrophobic, with 8 of its 10 phenylalanine side chains packed in an approximate herringbone pattern. 52 of the 108 residues are in six alpha-helixes; there is no beta-pleated sheet. The acetylated amino-terminal alanine appears not to be accessible to solvent. All of the heavy-atom derivatives are bound at the sole cysteine. The properties of this protein suggest a relationship to troponin A of mammalian tissue.Keywords
This publication has 10 references indexed in Scilit:
- Faculty Opinions recommendation of A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing.Published by H1 Connect ,2012
- Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for FoldingProceedings of the National Academy of Sciences of the United States of America, 1971
- Crystal data for low molecular weight albumins of carpJournal of Molecular Biology, 1971
- Reconstitution of Troponin Activity from Three Protein ComponentsJournal of Biological Chemistry, 1971
- Troponin and Its Components*The Journal of Biochemistry, 1971
- Control of muscle contractionQuarterly Reviews of Biophysics, 1969
- Studies on troponinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- CARP MYOGENS OF WHITE AND RED MUSCLES. PROPERTIES AND AMINO ACID COMPOSITION OF THE MAIN LOW-MOLECULAR-WEIGHT COMPONENTS OF WHITE MUSCLEBiochemical Journal, 1965
- CARP MYOGENS OF WHITE AND RED MUSCLES. GROSS ISOLATION ON SEPHADEX COLUMNS OF THE LOW-MOLECULAR-WEIGHT COMPONENTS AND EXAMINATION OF THEIR PARTICIPATION IN ANAEROBIC GLYCOGENOLYSISBiochemical Journal, 1965
- CARP MYOGENS OF WHITE AND RED MUSCLES. GENERAL COMPOSITION AND ISOLATION OF LOW-MOLECULAR-WEIGHT COMPONENTS OF ABNORMAL AMINO ACID COMPOSITIONBiochemical Journal, 1965