1CTA

DETERMINATION OF THE SOLUTION STRUCTURE OF A SYNTHETIC TWO-SITE CALCIUM-BINDING HOMODIMERIC PROTEIN DOMAIN BY NMR SPECTROSCOPY

Summary for 1CTA

• Entry DOI: 10.2210/pdb1cta/pdb
• Descriptor: TROPONIN C SITE III - SITE III HOMODIMER, CALCIUM ION (2 entities in total)
• Functional Keywords: muscle protein
• Total number of polymer chains: 2
• Total formula weight: 7792.62

Authors

Shaw, G.S.,Sykes, B.D. (deposition date: 1992-11-12, release date: 1993-10-31, Last modification date: 2024-10-23)

Primary citation

Shaw, G.S.,Hodges, R.S.,Sykes, B.D.
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Biochemistry, 31:9572-9580, 1992

PubMed Abstract: The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium this peptide forms a symmetric two-site homodimeric calcium-binding domain (Shaw et al., 1990). The solution structure of this dimer was determined from the measurement of 470 NOEs from a 75-ms NOESY data set. For the dimer structure determination, the constraint list included 868 distance restraints, 44 phi angles, and 24 chi 1 and 2 chi 2 angles. Seven structures were calculated by restrained molecular dynamics using a procedure in which intramonomer distances were used first and then all distances, intra- and intermonomer, were input during further dynamics. The structures exhibited a fold very similar to the C-terminal domain of troponin-C comprised of a pair of helix-loop-helix calcium-binding sites. The rms deviation of these structures for backbone atoms between residues 97-122 and 97'-122' for the dimer was 0.82 A. The dimer structure was also calculated to be more symmetric than sites III and IV in troponin-C.

PubMed: 1390738
DOI: 10.1021/bi00155a009

Experimental method

SOLUTION NMR