Biochemical and Biophysical Research Communications
Infrared spectroscopic study of the metal-coordination structures of calcium-binding proteins
Section snippets
Pike parvalbumin pI 4.10
Parvalbumins, which are ubiquitous in vertebrates, form a group in Ca2+-binding proteins in parallel with calmodulin and troponin C [30]. Although the function of parvalbumins is not yet understood, their involvement in the relaxation process of fast muscles has been proposed [31], [32]. Kretsinger and Nockolds [33] first reported the three-dimensional structure of carp parvalbumin (isoform pI 4.25) in crystal. According to their results, which Moew and Kretsinger later refined [34], this
Calmodulin
Calmodulin regulates the functions of a wide variety of enzymes [31], [32], [39]. It has four Ca2+-binding sites (I–IV). X-ray analyses [40], [41] have revealed that these four sites are similar to the EF-hand motif reported on parvalbumin [33], and that the COO− groups of Asp and Glu, the CONH2 groups of Asn and so on are coordinated to Ca2+. Bovine CaM has 17 Asp COO− groups and 21 Glu COO− groups in a molecule. Of these 38 COO− groups, 16 exist in the Ca2+-binding sites, and the COO− groups
Akazara scallop troponin C
Muscle contraction of vertebrate skeletal and cardiac muscles is regulated by troponin in a Ca2+-dependent manner [54]. Troponin contains three components: troponin C (TnC), troponin I and troponin T; TnC is the Ca2+-binding component. In general, TnC contains two independent Ca2+-binding domains, each consisting of two EF-hand motifs [55]. Vertebrate TnCs bind three or four Ca2+ ions in a molecule [56], [57], [58] and act as the Ca2+ switch of muscle contraction associated with the binding and
Synthetic peptide analogues of Ca2+-binding site: site IV of Akazara scallop TnC and site III of rabbit skeletal muscle TnC
The use of the synthetic calcium-binding peptide approach has provided valuable results for understanding the calcium-binding properties thus far [72], [73], [74], [75]. Calcium binding to a series of peptides derived from site III of rabbit skeletal muscle TnC has been studied by Reid et al. [72], who found that a 34-residue peptide was required for relatively tight calcium binding. Shorter peptides have decreased calcium affinity, and the isolated 12-residue Ca2+-binding loop binds to Ca2+
Concluding remarks
FTIR spectroscopy is a powerful tool for identifying the coordination structures of M2+ in Ca2+-binding proteins—that is, the coordination structure modes of side-chain COO− groups. The downshift of the COO− antisymmetric stretching mode from 1565 cm−1 to 1555–1540 cm−1 upon Ca2+ binding is a commonly observed feature of FTIR spectra for EF-hand proteins. Apart from the proteins described here, FTIR spectroscopy has already been successfully applied to other EF-hand proteins: recoverin [78],
Acknowledgments
This work was supported by the 21st Century Center of Excellence Program and by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan.
References (81)
- et al.
Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
J. Mol. Biol.
(1991) - et al.
Relationships between the carbon–oxygen stretching frequencies of carboxylato complexes and the type of carboxylate coordination
Coord. Chem. Rev.
(1980) - et al.
New insight into protein secondary structure from resolution-enhanced infrared-spectra
Biochim. Biophys. Acta
(1988) - et al.
Fourier-transform infrared spectroscopic studies of lipids, polypeptides and proteins
J. Mol. Struct.
(1989) The infrared absorption of amino acid side chains
Prog. Biophys. Mol. Biol.
(2000)- et al.
Infrared studies of interaction between metal ions and Ca2+-binding proteins. Marker bands for identifying the types of coordination of the side-chain COO− groups to metal ions in pike parvalbumin (pI = 4.10)
FEBS Lett.
(1994) - et al.
Infrared spectroscopic study on Ca2+ binding to Akazara scallop troponin C in comparison with peptide analogues if its Ca2+-binding site IV
Vib. Spectrosc.
(2006) - et al.
Calmodulin
Adv. Protein Chem.
(1982) - et al.
Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments
J. Biol. Chem.
(1973) - et al.
Refinement structure of carp muscle calcium-binding parvalbumin by model-building and difference Fourier-analysis
J. Mol. Biol.
(1975)
New solid-phase chelator with high affinity and selectivity for calcium–parvalbumin–polyacrylamide
Anal. Biochem.
Crystal-structure determination and refinement of pike 4.10 parvalbumin (minor component esox-lucius)
J. Mol. Biol.
Structure of calmodulin refined at 2.2 Å resolution
J. Mol. Biol.
Ca2+-binding and conformational change in two series of point mutations to the individual Ca2+-binding sites of calmodulin
J. Biol. Chem.
Divalent cation binding properties of bovine brain Ca2+-dependent regulator protein
J. Biol. Chem.
Effects of calcium and calcium analogues of calmodulin: a Fourier transform infrared and electron spin resonance investigation
Biochem. Biophys. Acta
Physicochemical properties of rat testis Ca2+-dependent regulator protein of cyclic nucleotide phosphodiesterase
J. Biol. Chem.
The amino acid sequence of rabbit skeletal muscle troponin C: gene replication and homology with calcium-binding proteins from carp and hake muscle
FEBS Lett.
The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
J. Biol. Chem.
The effect of Mg2+ on the Ca2+ binding to troponin C in rabbit fast skeletal myofibrils
Biochim. Biophys. Acta
Calcium
Curr. Opin. Chem. Biol.
Troponin from Akazara scallop striated adductor muscles
J. Biol. Chem.
Akazara scallop troponin C: Ca2+-induced conformational change and interaction with rabbit troponin subunits
Arch. Biochem. Biophys.
When size is important. Accommodation of magnesium in a calcium binding regulatory domain
J. Biol. Chem.
Calcium-induced protein folding
J. Biol. Chem.
Structures of four Ca2+-bound troponin C at 2.0 angstrom resolution: further insights into the Ca2+-switch in the calmodulin superfamily
Structure
The interaction of cyclic nucleotides and calcium in the control of cellular activity
Adv. Cyclic Nucleotide Res.
Calmodulin-a versatile calcium medicated protein
Biochem. Cell. Biol.
Ca2+ signaling and intracellular Ca2+ binding proteins
J. Biochem.
Coordination chemistry of alkali and alkaline earth cations
Chem. Rev.
Structure of the regulatory domain of scallop myosin at 2 Å resolution: implications for regulation
Structure
FT-IR characterization of metal acetates in aqueous-solution
Appl. Spectrosc.
Correlation between the vibrational frequencies of the carboxylate group and the types of its coordination to a metal ion: an ab initio molecular orbital study
J. Phys. Chem.
Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
Prog. Biophys. Mol. Biol.
Examination of the secondary structure of proteins by deconvolved FTIR spectra
Biopolymers
Determination of protein secondary structure by Fourier-transform infrared-spectroscopy. A critical assessment
Biochemistry
Fourier self-deconvolution- a method for resolving intrinsically overlapped bands
Appl. Spectrosc.
Cited by (73)
Potential dietary calcium supplement: Calcium-chelating peptides and peptide-calcium complexes derived from blue food proteins
2024, Trends in Food Science and TechnologyFacile metal-ion infiltration into polyimide membranes with coordination crosslinking for efficient gas separation
2023, Separation and Purification Technology