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Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution.

Swain AL, Kretsinger RH, Amma EL
J Biol Chem 264 16620-8 (1989)
Cited: 59 times
EuropePMC logo PMID: 2777802

Abstract

Carp parvalbumin coordinates calcium through one carbonyl oxygen atom and the oxygen-containing side chains of 5 amino acid residues, or 4 residues and a water molecule, in a helix-loop-helix structural motif. Other calcium-binding proteins, including calmodulin and troponin C, also possess this unique calcium-binding design, which is designated EF-hand or calmodulin fold. Parvalbumin has two such sites, labeled CD and EF. Each of the calcium-binding sites of refined structures of proteins belonging to this group has a 7-oxygen coordination sphere except those of the structure of parvalbumin as it was reported in 1975. This structure had been refined at 1.9 A using difference Fourier techniques on film data. The CD site appeared to be 6-coordinate and the EF site 8-coordinate. Results of NMR experiments using 113Cd-substituted parvalbumin, however, indicate that the sites are similar to one another with coordination number greater than 6. To resolve the inconsistency between crystallographic and NMR results, 1.6 A area detector data was collected for native and cadmium-substituted parvalbumin; the structures have been refined to R factors of 18.7% and 16.4%, respectively, with acceptable geometry and low errors in atomic coordinates. Differences between the parvalbumin structure described in 1975 and the present structure are addressed, including the discovery of 7-coordination for both the CD and EF sites.

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Related citations provided by authors (13)

  1. The Coordination Polyhedron of Ca2+,Cd2+ in Parvalbumin. Swain AL, Amma EL Inorganica Chim Acta 163 5- (1989)
  2. Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis.. Moews PC, Kretsinger RH J Mol Biol 91 201-25 (1975)
  3. Terbium Replacement of Calcium in Carp Muscle Calcium-Binding Parvalbumin,an X-Ray Crystallographic Study. Moews PC, Kretsinger RH J. Mol. Biol. 91 229- (1975)
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  5. Calcium Binding Proteins and Natural Membranes. Kretsinger RH Perspectives in Membrane Biology 229- (1974)
  6. The Coordination of Calcium Ions by Carp Muscle Calcium-Binding Proteins A,B,and C. Coffee CJ, Bradshaw RA, Kretsinger RH Adv. Exp. Med. Biol. 48 211- (1974)
  7. Carp Muscle Calcium-Binding Protein, I.Characterization of the Tryptic Peptides and the Complete Amino Acid Sequence of Component B. Coffee CJ, Bradshaw RA J. Biol. Chem. 248 3305- (1973)
  8. Carp Muscle Calcium-Binding Protein, II.Structure Determination and General Description. Kretsinger RH, Nockolds CE J. Biol. Chem. 248 3313- (1973)
  9. Carp Muscle Calcium-Binding Protein, III.Phase Refinement Using the Tangent Formula. Hendrickson WA, Karle J J. Biol. Chem. 248 3327- (1973)
  10. Gene duplication in carp muscle calcium binding protein.. McLachlan AD Nat New Biol 240 83-5 (1972)
  11. Gene triplication deduced from the tertiary structure of a muscle calcium binding protein.. Kretsinger RH Nat New Biol 240 85-8 (1972)
  12. Structure of a Calcium Binding Carp Myogen. Nockolds CE, Kretsinger RH, Coffee CJ, Bradshaw RA Proc. Natl. Acad. Sci. U.S.A. 69 581- (1972)
  13. The structure of a calcium-binding protein from carp muscle.. Kretsinger RH, Nockolds CE, Coffee CJ, Bradshaw RA Cold Spring Harb Symp Quant Biol 36 217-20 (1972)

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